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Conserved domains on  [gi|1807799449|ref|NP_001365277|]
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histone-arginine methyltransferase METTL23 isoform 1 [Homo sapiens]

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; ...
 3-126 8.01e-19

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: 79.30  E-value: 8.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449   3 VWPCAVVLAQYL------WFHRRSLPGKAILEIGAGVSLPGILAAK--CGAEVILSDSSELPHCLEvcrQSCQMNNL-PH 73
Cdd:pfam10294  21 VWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITDLEEALELLK---KNIELNALsSK 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1807799449  74 LQVVGLTWGH-ISWDLLALPPQDIILASDVFFEPEDFEDILATIYFLMHKNPKV 126
Cdd:pfam10294  98 VVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVI 151
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 3-126 8.01e-19

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: 79.30  E-value: 8.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449   3 VWPCAVVLAQYL------WFHRRSLPGKAILEIGAGVSLPGILAAK--CGAEVILSDSSELPHCLEvcrQSCQMNNL-PH 73
Cdd:pfam10294  21 VWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITDLEEALELLK---KNIELNALsSK 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1807799449  74 LQVVGLTWGH-ISWDLLALPPQDIILASDVFFEPEDFEDILATIYFLMHKNPKV 126
Cdd:pfam10294  98 VVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVI 151
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 15-117 6.47e-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: 46.55  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449  15 WFHRRSLPGKAILEIGAGvslPGILA---AKCGAEVILSDSSelPHCLEVCRQscqmnnlpHLQVVGLTWGHISWDLLAL 91
Cdd:COG2227    17 LLARLLPAGGRVLDVGCG---TGRLAlalARRGADVTGVDIS--PEALEIARE--------RAAELNVDFVQGDLEDLPL 83

                          90       100
                  ....*....|....*....|....*...
gi 1807799449  92 PPQ--DIILASDVFFEPEDFEDILATIY 117
Cdd:COG2227    84 EDGsfDLVICSEVLEHLPDPAALLRELA 111
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 26-120 7.95e-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: 34.71  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449  26 ILEIGAGVSLPGILAAK-CGAEVILSDSSelPHCLEVCRQSCQMNNLPHLQVVGLTWGHisWDLLALPPQDIILASDVF- 103
Cdd:cd02440     2 VLDLGCGTGALALALASgPGARVTGVDIS--PVALELARKAAAALLADNVEVLKGDAEE--LPPEADESFDVIISDPPLh 77

                          90
                  ....*....|....*..
gi 1807799449 104 FEPEDFEDILATIYFLM 120
Cdd:cd02440    78 HLVEDLARFLEEARRLL 94
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 3-126 8.01e-19

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: 79.30  E-value: 8.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449   3 VWPCAVVLAQYL------WFHRRSLPGKAILEIGAGVSLPGILAAK--CGAEVILSDSSELPHCLEvcrQSCQMNNL-PH 73
Cdd:pfam10294  21 VWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITDLEEALELLK---KNIELNALsSK 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1807799449  74 LQVVGLTWGH-ISWDLLALPPQDIILASDVFFEPEDFEDILATIYFLMHKNPKV 126
Cdd:pfam10294  98 VVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESVI 151
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 15-117 6.47e-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: 46.55  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449  15 WFHRRSLPGKAILEIGAGvslPGILA---AKCGAEVILSDSSelPHCLEVCRQscqmnnlpHLQVVGLTWGHISWDLLAL 91
Cdd:COG2227    17 LLARLLPAGGRVLDVGCG---TGRLAlalARRGADVTGVDIS--PEALEIARE--------RAAELNVDFVQGDLEDLPL 83

                          90       100
                  ....*....|....*....|....*...
gi 1807799449  92 PPQ--DIILASDVFFEPEDFEDILATIY 117
Cdd:COG2227    84 EDGsfDLVICSEVLEHLPDPAALLRELA 111
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 26-117 2.90e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.09  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449  26 ILEIGAGvslPGI----LAAKCGAEVILSDSSelPHCLEVCRQSCQMNNLPHLQVVGltwghiswDLLALPPQ----DII 97
Cdd:pfam13649   1 VLDLGCG---TGRltlaLARRGGARVTGVDLS--PEMLERARERAAEAGLNVEFVQG--------DAEDLPFPdgsfDLV 67

                          90       100
                  ....*....|....*....|..
gi 1807799449  98 LASDVF--FEPEDFEDILATIY 117
Cdd:pfam13649  68 VSSGVLhhLPDPDLEAALREIA 89
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
22-117 1.54e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.12  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449  22 PGKAILEIGAGvslPGILAAK-----CGAEVILSDSSelPHCLEVCRQscqmnNLPHLQVvgltwghISWDLLALPPQ-- 94
Cdd:COG4106     1 PPRRVLDLGCG---TGRLTALlaerfPGARVTGVDLS--PEMLARARA-----RLPNVRF-------VVADLRDLDPPep 63

                          90       100
                  ....*....|....*....|....
gi 1807799449  95 -DIILASDVFFEPEDFEDILATIY 117
Cdd:COG4106    64 fDLVVSNAALHWLPDHAALLARLA 87
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 22-117 1.81e-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: 36.90  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449  22 PGKAILEIGAGVSLPGILAAKCGAEVILSDSSelPHCLEVCRQscqmnnlpHLQVVGLTWGHISWDLLALPPQ----DII 97
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERGARVTGVDIS--PEMLELARE--------RAAEAGLNVEFVVGDAEDLPFPdgsfDLV 91

                          90       100
                  ....*....|....*....|
gi 1807799449  98 LASDVFFEPEDFEDILATIY 117
Cdd:COG2226    92 ISSFVLHHLPDPERALAEIA 111
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 26-120 7.95e-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: 34.71  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449  26 ILEIGAGVSLPGILAAK-CGAEVILSDSSelPHCLEVCRQSCQMNNLPHLQVVGLTWGHisWDLLALPPQDIILASDVF- 103
Cdd:cd02440     2 VLDLGCGTGALALALASgPGARVTGVDIS--PVALELARKAAAALLADNVEVLKGDAEE--LPPEADESFDVIISDPPLh 77

                          90
                  ....*....|....*..
gi 1807799449 104 FEPEDFEDILATIYFLM 120
Cdd:cd02440    78 HLVEDLARFLEEARRLL 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
2-117 9.98e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 35.36  E-value: 9.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807799449   2 YVWPcAVVLAQYLWFHRrSLPGKAILEIGAGVSLPGILAAKCGAEVILSDSSELPhcLEVCRQSCQMNNLPHLQVVGLTW 81
Cdd:COG4976    28 YEAP-ALLAEELLARLP-PGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEM--LAKAREKGVYDRLLVADLADLAE 103

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1807799449  82 GHISWDLlalppqdiILASDVFFEPEDFEDILATIY 117
Cdd:COG4976   104 PDGRFDL--------IVAADVLTYLGDLAAVFAGVA 131
 
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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