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Conserved domains on  [gi|1333087199|ref|XP_023521985|]
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methyltransferase-like protein 25 isoform X1 [Cucurbita pepo subsp. pepo]

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; ...
131-322 6.15e-26

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 pfam13679:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 138  Bit Score: 103.03  E-value: 6.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333087199 131 KKKHEVEVLSAIISLIASDLKSH----AIVDVGAGQVTLTFItvckmaqVLSFHYKHSVLAIDACSHHGNVTSARSERik 206
Cdd:pfam13679   1 KKLHQVEHLAEFIAPLLKELLDEngpiTIVDHGAGKGYLGFI-------LYYLKYGVRVYGIDTRAELVEKANALAQK-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333087199 207 kyysaqirksgletnnLRLPKAMTFHVLSVdalkslanmslqddhADKTSVTGDDlektnrqeskglcrsgkePSLVLAG 286
Cdd:pfam13679  72 ----------------LGFNKRMSFLEGTI---------------AGSTPVELPD------------------RVDVVTA 102
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1333087199 287 LHACGDLSVIMLRTFVeCKEVKAVINIGCCYNLLSE 322
Cdd:pfam13679 103 LHACDTATDDALRFAL-AKQARAIVLVPCCYHELAE 137
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
131-322 6.15e-26

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 103.03  E-value: 6.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333087199 131 KKKHEVEVLSAIISLIASDLKSH----AIVDVGAGQVTLTFItvckmaqVLSFHYKHSVLAIDACSHHGNVTSARSERik 206
Cdd:pfam13679   1 KKLHQVEHLAEFIAPLLKELLDEngpiTIVDHGAGKGYLGFI-------LYYLKYGVRVYGIDTRAELVEKANALAQK-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333087199 207 kyysaqirksgletnnLRLPKAMTFHVLSVdalkslanmslqddhADKTSVTGDDlektnrqeskglcrsgkePSLVLAG 286
Cdd:pfam13679  72 ----------------LGFNKRMSFLEGTI---------------AGSTPVELPD------------------RVDVVTA 102
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1333087199 287 LHACGDLSVIMLRTFVeCKEVKAVINIGCCYNLLSE 322
Cdd:pfam13679 103 LHACDTATDDALRFAL-AKQARAIVLVPCCYHELAE 137
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
131-322 6.15e-26

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 103.03  E-value: 6.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333087199 131 KKKHEVEVLSAIISLIASDLKSH----AIVDVGAGQVTLTFItvckmaqVLSFHYKHSVLAIDACSHHGNVTSARSERik 206
Cdd:pfam13679   1 KKLHQVEHLAEFIAPLLKELLDEngpiTIVDHGAGKGYLGFI-------LYYLKYGVRVYGIDTRAELVEKANALAQK-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333087199 207 kyysaqirksgletnnLRLPKAMTFHVLSVdalkslanmslqddhADKTSVTGDDlektnrqeskglcrsgkePSLVLAG 286
Cdd:pfam13679  72 ----------------LGFNKRMSFLEGTI---------------AGSTPVELPD------------------RVDVVTA 102
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1333087199 287 LHACGDLSVIMLRTFVeCKEVKAVINIGCCYNLLSE 322
Cdd:pfam13679 103 LHACDTATDDALRFAL-AKQARAIVLVPCCYHELAE 137
 
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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