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Conserved domains on  [gi|18401209|ref|NP_565628|]
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FkbM family methyltransferase [Arabidopsis thaliana]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
134-279 3.26e-28

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.).


The actual alignment was detected with superfamily member TIGR01444:

Pssm-ID: 473071  Cd Length: 143  Bit Score: 106.24  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   134 IVVDVGANVGMAS--FAAAVMGFKVLAFEPVFENLQRICDGIWFNRVaSLVTVFEAAASDRTGDITFHKLVGRLDNSAVS 211
Cdd:TIGR01444   1 VVIDVGANIGDTSlyFARKGAEGRVIAFEPLPDAYEILEENVKLNNL-PNVVLLNAAVGDRDGELEFNVSDDDTGNSSLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   212 EVGARlafksNKEIAVQVKSIPLDKLIP--PSQPVLLIKIDVQGWEYHVLKGAKKLLSGKpaeAPYLIYE 279
Cdd:TIGR01444  80 PTPDA-----DRESEIEVEVVTLDDLVEefGLDKVDLLKIDVEGAELEVLRGAAETLLEK---RPVIVLE 141
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
134-279 3.26e-28

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 106.24  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   134 IVVDVGANVGMAS--FAAAVMGFKVLAFEPVFENLQRICDGIWFNRVaSLVTVFEAAASDRTGDITFHKLVGRLDNSAVS 211
Cdd:TIGR01444   1 VVIDVGANIGDTSlyFARKGAEGRVIAFEPLPDAYEILEENVKLNNL-PNVVLLNAAVGDRDGELEFNVSDDDTGNSSLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   212 EVGARlafksNKEIAVQVKSIPLDKLIP--PSQPVLLIKIDVQGWEYHVLKGAKKLLSGKpaeAPYLIYE 279
Cdd:TIGR01444  80 PTPDA-----DRESEIEVEVVTLDDLVEefGLDKVDLLKIDVEGAELEVLRGAAETLLEK---RPVIVLE 141
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
137-304 2.89e-18

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 80.69  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   137 DVGANVGMASFAAAVM------GFKVLAFEPVFENLQRICDgiwfnrvaslvTVFEAAASDRTGDITFH----KLVGRLD 206
Cdd:pfam05050   1 DVGANDGVWDSVALLFekkcggGGEVLAIEPNPNKLEKLDC-----------TLLNLALGNDVGLYEFYlggkGGGGYLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   207 NSAVSEVGARLAFKSNKEIAVQVK--SIPLDKLIPPSQP--VLLIKIDVQGWEYHVLKGAKKLLSgkpAEAPYLIYEEDE 282
Cdd:pfam05050  70 FAVGDPQGASTSSVLGGEEAKYIEveTVTLDSFLEEIKKsdIDLLKIDVEGAELEVLEGAEKTLK---RCQPNIIVIEVH 146
                         170       180
                  ....*....|....*....|..
gi 18401209   283 RLLTASNSSSKEIRDFLKSVGY 304
Cdd:pfam05050 147 FFHYFGGPLFDEIRQFLRECGY 168
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
134-279 3.26e-28

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 106.24  E-value: 3.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   134 IVVDVGANVGMAS--FAAAVMGFKVLAFEPVFENLQRICDGIWFNRVaSLVTVFEAAASDRTGDITFHKLVGRLDNSAVS 211
Cdd:TIGR01444   1 VVIDVGANIGDTSlyFARKGAEGRVIAFEPLPDAYEILEENVKLNNL-PNVVLLNAAVGDRDGELEFNVSDDDTGNSSLL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   212 EVGARlafksNKEIAVQVKSIPLDKLIP--PSQPVLLIKIDVQGWEYHVLKGAKKLLSGKpaeAPYLIYE 279
Cdd:TIGR01444  80 PTPDA-----DRESEIEVEVVTLDDLVEefGLDKVDLLKIDVEGAELEVLRGAAETLLEK---RPVIVLE 141
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
137-304 2.89e-18

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 80.69  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   137 DVGANVGMASFAAAVM------GFKVLAFEPVFENLQRICDgiwfnrvaslvTVFEAAASDRTGDITFH----KLVGRLD 206
Cdd:pfam05050   1 DVGANDGVWDSVALLFekkcggGGEVLAIEPNPNKLEKLDC-----------TLLNLALGNDVGLYEFYlggkGGGGYLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401209   207 NSAVSEVGARLAFKSNKEIAVQVK--SIPLDKLIPPSQP--VLLIKIDVQGWEYHVLKGAKKLLSgkpAEAPYLIYEEDE 282
Cdd:pfam05050  70 FAVGDPQGASTSSVLGGEEAKYIEveTVTLDSFLEEIKKsdIDLLKIDVEGAELEVLEGAEKTLK---RCQPNIIVIEVH 146
                         170       180
                  ....*....|....*....|..
gi 18401209   283 RLLTASNSSSKEIRDFLKSVGY 304
Cdd:pfam05050 147 FFHYFGGPLFDEIRQFLRECGY 168
 
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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