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Conserved domains on  [gi|568906659|ref|XP_006496189|]
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protein-lysine methyltransferase METTL21C isoform X1 [Mus musculus]

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; ...
 56-224 3.41e-31

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: 113.20  E-value: 3.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659   56 QFAGKKIIIQESIEN-YGTVVWPGATALCQYLE----DHTEELNLQDAKILEIGAGAGLVSIVSSLL--GAQVTATDLPD 128
Cdd:pfam10294   1 KLDNPGLRIEEDTGNgIGGHVWDAAVVLSKYLEmkifKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  129 VLGNLQYNILKNTLECTAHlpeVRELVWGEDLEQSFPKSTCcYDYVLASDVVYHHYFLDKLLATMVYLSQPGTVVLWANK 208
Cdd:pfam10294  81 ALELLKKNIELNALSSKVV---VKVLDWGENLPPDLFDGHP-VDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYK 156

                         170
                  ....*....|....*.
gi 568906659  209 FRFSADYEFLGKFKQA 224
Cdd:pfam10294 157 KRREAEKKFFKLLERF 172
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 56-224 3.41e-31

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: 113.20  E-value: 3.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659   56 QFAGKKIIIQESIEN-YGTVVWPGATALCQYLE----DHTEELNLQDAKILEIGAGAGLVSIVSSLL--GAQVTATDLPD 128
Cdd:pfam10294   1 KLDNPGLRIEEDTGNgIGGHVWDAAVVLSKYLEmkifKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  129 VLGNLQYNILKNTLECTAHlpeVRELVWGEDLEQSFPKSTCcYDYVLASDVVYHHYFLDKLLATMVYLSQPGTVVLWANK 208
Cdd:pfam10294  81 ALELLKKNIELNALSSKVV---VKVLDWGENLPPDLFDGHP-VDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYK 156

                         170
                  ....*....|....*.
gi 568906659  209 FRFSADYEFLGKFKQA 224
Cdd:pfam10294 157 KRREAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 80-204 1.73e-08

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: 51.56  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  80 TALCQYLEDHTeelnLQDAKILEIGAGAGLVSIVSSLLGAQVTATDL-PDVLGNLQynilkntlectAHLPEVRELVWGE 158
Cdd:COG2227   12 RRLAALLARLL----PAGGRVLDVGCGTGRLALALARRGADVTGVDIsPEALEIAR-----------ERAAELNVDFVQG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568906659 159 DLEQsFPKSTCCYDYVLASDVVYHHYFLDKLLATMVYLSQPGTVVL 204
Cdd:COG2227   77 DLED-LPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLL 121
PRK14968 PRK14968
putative methyltransferase; Provisional
 99-126 9.49e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 9.49e-04
                         10        20
                 ....*....|....*....|....*...
gi 568906659  99 KILEIGAGAGLVSIVSSLLGAQVTATDL 126
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 99-204 4.62e-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: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  99 KILEIGAGAGLVSI-VSSLLGAQVTATDL-PDVLGNLQYNILKNTLECTahlpEVRELVWGEDLEQSFPKstccYDYVLa 176
Cdd:cd02440    1 RVLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNV----EVLKGDAEELPPEADES----FDVII- 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 568906659 177 SDVVYHHYFLD--KLLATMVYLSQPGTVVL 204
Cdd:cd02440   72 SDPPLHHLVEDlaRFLEEARRLLKPGGVLV 101
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 92-143 6.13e-03

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 36.76  E-value: 6.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906659   92 ELNLQDAK---ILEIGAGAGLVSIVSSLLGAQVTATDL-PDVLGNLQYNILKNTLE 143
Cdd:TIGR00537  12 EANLRELKpddVLEIGAGTGLVAIRLKGKGKCILTTDInPFAVKELRENAKLNNVG 67
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 56-224 3.41e-31

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: 113.20  E-value: 3.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659   56 QFAGKKIIIQESIEN-YGTVVWPGATALCQYLE----DHTEELNLQDAKILEIGAGAGLVSIVSSLL--GAQVTATDLPD 128
Cdd:pfam10294   1 KLDNPGLRIEEDTGNgIGGHVWDAAVVLSKYLEmkifKELGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  129 VLGNLQYNILKNTLECTAHlpeVRELVWGEDLEQSFPKSTCcYDYVLASDVVYHHYFLDKLLATMVYLSQPGTVVLWANK 208
Cdd:pfam10294  81 ALELLKKNIELNALSSKVV---VKVLDWGENLPPDLFDGHP-VDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAYK 156

                         170
                  ....*....|....*.
gi 568906659  209 FRFSADYEFLGKFKQA 224
Cdd:pfam10294 157 KRREAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 80-204 1.73e-08

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: 51.56  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  80 TALCQYLEDHTeelnLQDAKILEIGAGAGLVSIVSSLLGAQVTATDL-PDVLGNLQynilkntlectAHLPEVRELVWGE 158
Cdd:COG2227   12 RRLAALLARLL----PAGGRVLDVGCGTGRLALALARRGADVTGVDIsPEALEIAR-----------ERAAELNVDFVQG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568906659 159 DLEQsFPKSTCCYDYVLASDVVYHHYFLDKLLATMVYLSQPGTVVL 204
Cdd:COG2227   77 DLED-LPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLL 121
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 38-140 1.34e-05

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: 45.33  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659   38 SIQKFVPTDYASYTQEHYQ--FAGKKIII----QESIENYGTVVW---PGA---------TALC-QYLEdhteELNLQDA 98
Cdd:pfam06325  88 TVEEVAEEDWARAWKKYFHpvRIGERLTIvpswEDYPENPDALNIeldPGMafgtgthptTKLClEALE----RLVKPGE 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568906659   99 KILEIGAGAGLVSIVSSLLGAQ-VTATDLPDV-LGNLQYNILKN 140
Cdd:pfam06325 164 SVLDVGCGSGILAIAALKLGAKkVVGVDIDPVaVRAAKENAELN 207
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 100-182 1.02e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 40.24  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  100 ILEIGAGAGLVSI-VSSLLGAQVTATDL-PDVLGNLQYNILKNTLECTAHLPEVRELvwgedleqSFPKSTccYDYVLAS 177
Cdd:pfam13649   1 VLDLGCGTGRLTLaLARRGGARVTGVDLsPEMLERARERAAEAGLNVEFVQGDAEDL--------PFPDGS--FDLVVSS 70


                  ....*
gi 568906659  178 DVVYH 182
Cdd:pfam13649  71 GVLHH 75
PRK14968 PRK14968
putative methyltransferase; Provisional
 99-126 9.49e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 9.49e-04
                         10        20
                 ....*....|....*....|....*...
gi 568906659  99 KILEIGAGAGLVSIVSSLLGAQVTATDL 126
Cdd:PRK14968  26 RVLEVGTGSGIVAIVAAKNGKKVVGVDI 53
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
96-194 2.91e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 36.34  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  96 QDAKILEIGAGAGLVS--IVSSLLGAQVTATDL-PDVLGnlqynilkntlECTAHLPEVRELVwgEDLEQSFPKSTccYD 172
Cdd:COG4106    1 PPRRVLDLGCGTGRLTalLAERFPGARVTGVDLsPEMLA-----------RARARLPNVRFVV--ADLRDLDPPEP--FD 65

                         90       100
                 ....*....|....*....|..
gi 568906659 173 YVLASDVVYHHYFLDKLLATMV 194
Cdd:COG4106   66 LVVSNAALHWLPDHAALLARLA 87
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 101-182 4.44e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.81  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  101 LEIGAGAG--LVSIVSSLLGAQVTATDL-PDVLGNLQYNILKNTLECTAHLpevrELVWGEDLEQSFPKstccYDYVLAS 177
Cdd:pfam08242   1 LEIGCGTGtlLRALLEALPGLEYTGLDIsPAALEAARERLAALGLLNAVRV----ELFQLDLGELDPGS----FDVVVAS 72


                  ....*
gi 568906659  178 DVVYH 182
Cdd:pfam08242  73 NVLHH 77
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 99-204 4.62e-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: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  99 KILEIGAGAGLVSI-VSSLLGAQVTATDL-PDVLGNLQYNILKNTLECTahlpEVRELVWGEDLEQSFPKstccYDYVLa 176
Cdd:cd02440    1 RVLDLGCGTGALALaLASGPGARVTGVDIsPVALELARKAAAALLADNV----EVLKGDAEELPPEADES----FDVII- 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 568906659 177 SDVVYHHYFLD--KLLATMVYLSQPGTVVL 204
Cdd:cd02440   72 SDPPLHHLVEDlaRFLEEARRLLKPGGVLV 101
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 92-143 6.13e-03

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 36.76  E-value: 6.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906659   92 ELNLQDAK---ILEIGAGAGLVSIVSSLLGAQVTATDL-PDVLGNLQYNILKNTLE 143
Cdd:TIGR00537  12 EANLRELKpddVLEIGAGTGLVAIRLKGKGKCILTTDInPFAVKELRENAKLNNVG 67
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 91-182 7.47e-03

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: 35.74  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906659  91 EELNLQ-DAKILEIGAGAGLVSIVSSLLGAQVTATDL-PDVLGNLQYNILKNTLECTAHLPEVRELvwgedleqsfPKST 168
Cdd:COG2226   16 AALGLRpGARVLDLGCGTGRLALALAERGARVTGVDIsPEMLELARERAAEAGLNVEFVVGDAEDL----------PFPD 85

                         90
                 ....*....|....
gi 568906659 169 CCYDYVLASDVVYH 182
Cdd:COG2226   86 GSFDLVISSFVLHH 99
 
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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