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Conserved domains on  [gi|500641587|ref|WP_011963710|]
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class I SAM-dependent methyltransferase [Flavobacterium psychrophilum]

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.
 45-131 2.55e-12

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 60.27  E-value: 2.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587   45 IIDIGAGDSHFIDALLDLGFTNLYLLDISAKAIERIQERLGEKSKNVTFIVSDI--LDFHSEiLFDFWHDRASFHFLTAE 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAedLPFPDG-SFDLVVSSGVLHHLPDP 79


                  ....*....
gi 500641587  123 DQIRKYAQI 131
Cdd:pfam13649  80 DLEAALREI 88
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 45-131 2.55e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 60.27  E-value: 2.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587   45 IIDIGAGDSHFIDALLDLGFTNLYLLDISAKAIERIQERLGEKSKNVTFIVSDI--LDFHSEiLFDFWHDRASFHFLTAE 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAedLPFPDG-SFDLVVSSGVLHHLPDP 79


                  ....*....
gi 500641587  123 DQIRKYAQI 131
Cdd:pfam13649  80 DLEAALREI 88
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
41-144 4.11e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 57.14  E-value: 4.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  41 KNAKIIDIGAGDSHFIDALLD-LGFTNLYLLDISAKAIERIQERLGekskNVTFIVSDILDFHSEILFDFWHDRASFHFL 119
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAErFPGARVTGVDLSPEMLARARARLP----NVRFVVADLRDLDPPEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....*
gi 500641587 120 taEDQIRKYAQIVsQSIAKKGKLVI 144
Cdd:COG4106   77 --PDHAALLARLA-AALAPGGVLAV 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 44-147 8.40e-10

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: 53.97  E-value: 8.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  44 KIIDIGAGDSHFIDALLDLGFTNLYLLDISAKAIERIQE-RLGEKSKNVTFIVSDILDFHSEIL--FDFWHDRASFHFLT 120
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEELPPEADesFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 500641587 121 AEdqIRKYAQIVSQSIAKKGKLVIGTF 147
Cdd:cd02440   81 ED--LARFLEEARRLLKPGGVLVLTLV 105
rADc smart00650
Ribosomal RNA adenine dimethylases;
33-102 3.78e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 36.72  E-value: 3.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587    33 FVKEFNLQKNAKIIDIGAGDSHFIDALLDLGFtNLYLLDISAKAIERIQERLGEKSkNVTFIVSDILDFH 102
Cdd:smart00650   5 IVRAANLRPGDTVLEIGPGKGALTEELLERAK-RVTAIEIDPRLAPRLREKFAAAD-NLTVIHGDALKFD 72
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 45-131 2.55e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 60.27  E-value: 2.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587   45 IIDIGAGDSHFIDALLDLGFTNLYLLDISAKAIERIQERLGEKSKNVTFIVSDI--LDFHSEiLFDFWHDRASFHFLTAE 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAedLPFPDG-SFDLVVSSGVLHHLPDP 79


                  ....*....
gi 500641587  123 DQIRKYAQI 131
Cdd:pfam13649  80 DLEAALREI 88
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
41-144 4.11e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 57.14  E-value: 4.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  41 KNAKIIDIGAGDSHFIDALLD-LGFTNLYLLDISAKAIERIQERLGekskNVTFIVSDILDFHSEILFDFWHDRASFHFL 119
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAErFPGARVTGVDLSPEMLARARARLP----NVRFVVADLRDLDPPEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....*
gi 500641587 120 taEDQIRKYAQIVsQSIAKKGKLVI 144
Cdd:COG4106   77 --PDHAALLARLA-AALAPGGVLAV 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 33-148 6.70e-11

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 57.70  E-value: 6.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  33 FVKEFNLQKNAKIIDIGAGDSHFIDALLDLGFTnLYLLDISAKAIERIQERLGEKSKNVTFIVSDI--LDFHSEIlFDFW 110
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVEFVVGDAedLPFPDGS-FDLV 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500641587 111 HDRASFHFLtaEDQIRKYAQIVsqSIAKK-GKLVIGTFS 148
Cdd:COG2226   92 ISSFVLHHL--PDPERALAEIA--RVLKPgGRLVVVDFS 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 39-144 4.20e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.85  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  39 LQKNAKIIDIGAGDSHFIDALLDLGFTNLYLLDISAKAIERIQERLGE-KSKNVTFIVSDILDFHSEIL--FDFWHDRAS 115
Cdd:COG0500   24 LPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKaGLGNVEFLVADLAELDPLPAesFDLVVAFGV 103

                         90       100
                 ....*....|....*....|....*....
gi 500641587 116 FHFLtAEDQIRKYAQIVSQSIAKKGKLVI 144
Cdd:COG0500  104 LHHL-PPEEREALLRELARALKPGGVLLL 131
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 44-147 8.40e-10

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: 53.97  E-value: 8.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  44 KIIDIGAGDSHFIDALLDLGFTNLYLLDISAKAIERIQE-RLGEKSKNVTFIVSDILDFHSEIL--FDFWHDRASFHFLT 120
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEELPPEADesFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 500641587 121 AEdqIRKYAQIVSQSIAKKGKLVIGTF 147
Cdd:cd02440   81 ED--LARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 41-174 2.96e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.88  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587   41 KNAKIIDIGAGDSHFIDALLDLGFTN--LYLLDISAKAIERIQERLGEK-SKNVTFIVSDILDFHSEIL---FDFWHDRA 114
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNaeVVGIDISEEAIEKARENAQKLgFDNVEFEQGDIEELPELLEddkFDVVISNC 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500641587  115 SFHFLTAEDQIrkyAQIVSQSIAKKGKLVIGTFS---------ENGPKKCSGLDIMQYSENKMNAIFEE 174
Cdd:pfam13847  83 VLNHIPDPDKV---LQEILRVLKPGGRLIISDPDslaelpahvKEDSTYYAGCVGGAILKKKLYELLEE 148
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 32-148 1.34e-07

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 48.48  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  32 NFVKEFnLQKNAKIIDIGAGDSHFIDALLDLGFtNLYLLDISAKAIERIQERLGEksKNVTFIVSDILDFHSE------- 104
Cdd:COG2227   16 ALLARL-LPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLEdgsfdlv 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 500641587 105 ILFDFWHdrasfHFLTAEDQIRKYAQIVsqsiAKKGKLVIGTFS 148
Cdd:COG2227   92 ICSEVLE-----HLPDPAALLRELARLL----KPGGLLLLSTPN 126
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 46-119 2.32e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 47.36  E-value: 2.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500641587   46 IDIGAGDSHFIDALLD-LGFTNLYLLDISAKAIERIQERLGEKS----KNVTFIVSDILDFHSEIlFDFWHDRASFHFL 119
Cdd:pfam08242   1 LEIGCGTGTLLRALLEaLPGLEYTGLDISPAALEAARERLAALGllnaVRVELFQLDLGELDPGS-FDVVVASNVLHHL 78
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
33-144 2.11e-04

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 40.37  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  33 FVKEFNLQKNAKIIDIGAGDSHFIDALLDLGFTnLYLLDISAKAIERIQERLGEksknVTFIVSDILDFHseilfdfWHD 112
Cdd:COG4976   38 LLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGVDLSEEMLAKAREKGVY----DRLLVADLADLA-------EPD 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 500641587 113 RA-----SFHFLTAEDQIRKYAQIVSQSIAKKGKLVI 144
Cdd:COG4976  106 GRfdlivAADVLTYLGDLAAVFAGVARALKPGGLFIF 142
rADc smart00650
Ribosomal RNA adenine dimethylases;
33-102 3.78e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 36.72  E-value: 3.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587    33 FVKEFNLQKNAKIIDIGAGDSHFIDALLDLGFtNLYLLDISAKAIERIQERLGEKSkNVTFIVSDILDFH 102
Cdd:smart00650   5 IVRAANLRPGDTVLEIGPGKGALTEELLERAK-RVTAIEIDPRLAPRLREKFAAAD-NLTVIHGDALKFD 72
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 38-146 6.37e-03

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 35.68  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587  38 NLQKNAKIIDIGAGdshfidalldLGFTNLYL----------LDISAKAIERIQERLGEK--SKNVTFIVSDILDFHSEI 105
Cdd:COG2230   48 GLKPGMRVLDIGCG----------WGGLALYLarrygvrvtgVTLSPEQLEYARERAAEAglADRVEVRLADYRDLPADG 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 500641587 106 LFDFWHDRASFHFLtAEDQIRKYAQIVSQSIAKKGKLVIGT 146
Cdd:COG2230  118 QFDAIVSIGMFEHV-GPENYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-147 8.79e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 35.48  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641587   37 FNLQKNAKIIDIGAGDSHFIDALLDLGFTNlYLLDISAKAIERIqerlGEKSKNVTFIVSDILDFHSEilFDFWHdraSF 116
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTGIFLRLLRAQGFSV-TGVDPSPIAIERA----LLNVRFDQFDEQEAAVPAGK--FDVIV---AR 87

                          90       100       110
                  ....*....|....*....|....*....|.
gi 500641587  117 HFLTAEDQIRKYAQIVSQSIAKKGKLVIGTF 147
Cdd:pfam13489  88 EVLEHVPDPPALLRQIAALLKPGGLLLLSTP 118
 
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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