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Conserved domains on  [gi|15241427|ref|NP_199230|]
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S-adenosyl-L-methionine-dependent methyltransferases superfamily protein [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; ...
14-192 1.74e-21

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 pfam10294:

Pssm-ID: 473071  Cd Length: 172  Bit Score: 87.39  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    14 NGTKLSIQQDNGSmHVGTSVWPCSLILSKFAERWSTLDSSSSttspnpyaelfDFRRRRGIELGTGCGVAGMAFYLLGL- 92
Cdd:pfam10294   3 DNPGLRIEEDTGN-GIGGHVWDAAVVLSKYLEMKIFKELGAN-----------NLSGLNVLELGSGTGLVGIAVALLLPg 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    93 TEIVLTDIAPVMPALKHNLKRNktALGKSLKTSIVYWNNRDQISALKP-PFDLVIAADVVYIEESVGQLVTAMELLVADD 171
Cdd:pfam10294  71 ASVTITDLEEALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLFDGhPVDLILAADCVYNEDSFPLLEKTLKDLLGKE 148
                         170       180
                  ....*....|....*....|.
gi 15241427   172 GAVLLGYQIRsPEADKLFWEL 192
Cdd:pfam10294 149 SVILVAYKKR-REAEKKFFKL 168
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
14-192 1.74e-21

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 87.39  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    14 NGTKLSIQQDNGSmHVGTSVWPCSLILSKFAERWSTLDSSSSttspnpyaelfDFRRRRGIELGTGCGVAGMAFYLLGL- 92
Cdd:pfam10294   3 DNPGLRIEEDTGN-GIGGHVWDAAVVLSKYLEMKIFKELGAN-----------NLSGLNVLELGSGTGLVGIAVALLLPg 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    93 TEIVLTDIAPVMPALKHNLKRNktALGKSLKTSIVYWNNRDQISALKP-PFDLVIAADVVYIEESVGQLVTAMELLVADD 171
Cdd:pfam10294  71 ASVTITDLEEALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLFDGhPVDLILAADCVYNEDSFPLLEKTLKDLLGKE 148
                         170       180
                  ....*....|....*....|.
gi 15241427   172 GAVLLGYQIRsPEADKLFWEL 192
Cdd:pfam10294 149 SVILVAYKKR-REAEKKFFKL 168
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
72-178 4.41e-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: 35.87  E-value: 4.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427  72 RGIELGTGCGVAGMAFYLLGLTEIVLTDIAPVMpaLKHNLKRNktALGKSLKTSIVYWNNRDQISALKPPFDLVIAADVV 151
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVA--LELARKAA--AALLADNVEVLKGDAEELPPEADESFDVIISDPPL 76
                        90       100
                ....*....|....*....|....*...
gi 15241427 152 -YIEESVGQLVTAMELLVADDGAVLLGY 178
Cdd:cd02440  77 hHLVEDLARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
14-192 1.74e-21

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 87.39  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    14 NGTKLSIQQDNGSmHVGTSVWPCSLILSKFAERWSTLDSSSSttspnpyaelfDFRRRRGIELGTGCGVAGMAFYLLGL- 92
Cdd:pfam10294   3 DNPGLRIEEDTGN-GIGGHVWDAAVVLSKYLEMKIFKELGAN-----------NLSGLNVLELGSGTGLVGIAVALLLPg 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    93 TEIVLTDIAPVMPALKHNLKRNktALGKSLKTSIVYWNNRDQISALKP-PFDLVIAADVVYIEESVGQLVTAMELLVADD 171
Cdd:pfam10294  71 ASVTITDLEEALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLFDGhPVDLILAADCVYNEDSFPLLEKTLKDLLGKE 148
                         170       180
                  ....*....|....*....|.
gi 15241427   172 GAVLLGYQIRsPEADKLFWEL 192
Cdd:pfam10294 149 SVILVAYKKR-REAEKKFFKL 168
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
79-172 2.03e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 39.27  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    79 GCGVAGMAFYLLGL---TEIVLTDIAPVMPALKhnlkRNKTALGKSLKTSIVYWNNRDQISALKPPFDLVIAADVV-YIE 154
Cdd:pfam08242   4 GCGTGTLLRALLEAlpgLEYTGLDISPAALEAA----RERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLhHLA 79
                          90
                  ....*....|....*...
gi 15241427   155 ESVGQLVTAMELLvADDG 172
Cdd:pfam08242  80 DPRAVLRNIRRLL-KPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
72-178 4.41e-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: 35.87  E-value: 4.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427  72 RGIELGTGCGVAGMAFYLLGLTEIVLTDIAPVMpaLKHNLKRNktALGKSLKTSIVYWNNRDQISALKPPFDLVIAADVV 151
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVA--LELARKAA--AALLADNVEVLKGDAEELPPEADESFDVIISDPPL 76
                        90       100
                ....*....|....*....|....*...
gi 15241427 152 -YIEESVGQLVTAMELLVADDGAVLLGY 178
Cdd:cd02440  77 hHLVEDLARFLEEARRLLKPGGVLVLTL 104
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
74-151 9.15e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 36.48  E-value: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241427    74 IELGTGCGVAGMAFYLLGLTEIVLTDIAPV-MPALKHNLKRNKTALGKSLKTSivywnnRDQisaLKPPFDLVIA---AD 149
Cdd:pfam06325 166 LDVGCGSGILAIAALKLGAKKVVGVDIDPVaVRAAKENAELNGVEARLEVYLP------GDL---PKEKADVVVAnilAD 236

                  ..
gi 15241427   150 VV 151
Cdd:pfam06325 237 PL 238
 
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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