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Conserved domains on  [gi|706716016|ref|NP_001289634|]
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histone-arginine methyltransferase METTL23 isoform 3 [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; ...
24-122 7.35e-11

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: 58.11  E-value: 7.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706716016   24 QIGAGVSLPGILAAK--CGAEVILSDSSELPHCLEvcrQSCQMNNL-PHLQVVGLTWGH-ISWDLLALPPQDIILASDVF 99
Cdd:pfam10294  52 ELGSGTGLVGIAVALllPGASVTITDLEEALELLK---KNIELNALsSKVVVKVLDWGEnLPPDLFDGHPVDLILAADCV 128
                          90       100
                  ....*....|....*....|...
gi 706716016  100 FEPEDFEDILATIYFLMHKNPKV 122
Cdd:pfam10294 129 YNEDSFPLLEKTLKDLLGKESVI 151
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
24-122 7.35e-11

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: 58.11  E-value: 7.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706716016   24 QIGAGVSLPGILAAK--CGAEVILSDSSELPHCLEvcrQSCQMNNL-PHLQVVGLTWGH-ISWDLLALPPQDIILASDVF 99
Cdd:pfam10294  52 ELGSGTGLVGIAVALllPGASVTITDLEEALELLK---KNIELNALsSKVVVKVLDWGEnLPPDLFDGHPVDLILAADCV 128
                          90       100
                  ....*....|....*....|...
gi 706716016  100 FEPEDFEDILATIYFLMHKNPKV 122
Cdd:pfam10294 129 YNEDSFPLLEKTLKDLLGKESVI 151
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
26-113 6.89e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 37.50  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706716016  26 GAGVSLPGILAAKCGAEVILSDSSelPHCLEVCRQscqmnNLPHLQVvgltwghISWDLLALPPQ---DIILASDVFFEP 102
Cdd:COG4106   11 GTGRLTALLAERFPGARVTGVDLS--PEMLARARA-----RLPNVRF-------VVADLRDLDPPepfDLVVSNAALHWL 76
                         90
                 ....*....|.
gi 706716016 103 EDFEDILATIY 113
Cdd:COG4106   77 PDHAALLARLA 87
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
24-122 7.35e-11

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: 58.11  E-value: 7.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706716016   24 QIGAGVSLPGILAAK--CGAEVILSDSSELPHCLEvcrQSCQMNNL-PHLQVVGLTWGH-ISWDLLALPPQDIILASDVF 99
Cdd:pfam10294  52 ELGSGTGLVGIAVALllPGASVTITDLEEALELLK---KNIELNALsSKVVVKVLDWGEnLPPDLFDGHPVDLILAADCV 128
                          90       100
                  ....*....|....*....|...
gi 706716016  100 FEPEDFEDILATIYFLMHKNPKV 122
Cdd:pfam10294 129 YNEDSFPLLEKTLKDLLGKESVI 151
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
25-113 3.99e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.93  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706716016   25 IGAGvslPGI----LAAKCGAEVILSDSSelPHCLEVCRQSCQMNNLPHLQVVGltwghiswDLLALPPQ----DIILAS 96
Cdd:pfam13649   4 LGCG---TGRltlaLARRGGARVTGVDLS--PEMLERARERAAEAGLNVEFVQG--------DAEDLPFPdgsfDLVVSS 70
                          90
                  ....*....|....*....
gi 706716016   97 DVF--FEPEDFEDILATIY 113
Cdd:pfam13649  71 GVLhhLPDPDLEAALREIA 89
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
26-113 6.89e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 37.50  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706716016  26 GAGVSLPGILAAKCGAEVILSDSSelPHCLEVCRQscqmnNLPHLQVvgltwghISWDLLALPPQ---DIILASDVFFEP 102
Cdd:COG4106   11 GTGRLTALLAERFPGARVTGVDLS--PEMLARARA-----RLPNVRF-------VVADLRDLDPPepfDLVVSNAALHWL 76
                         90
                 ....*....|.
gi 706716016 103 EDFEDILATIY 113
Cdd:COG4106   77 PDHAALLARLA 87
 
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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