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Conserved domains on  [gi|1034613500|ref|XP_016859438|]
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histamine N-methyltransferase isoform X3 [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; ...
 32-148 4.20e-09

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 pfam13489:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 162  Bit Score: 52.43  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613500  32 MQEFMDKKLPGIIGRIGDT-KSEIKILSIGGGAGeIDLQILSKVQAQYPGVCINNEVVEPsaeqiakykelvaktsNLEN 110
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKlPSPGRVLDFGCGTG-IFLRLLRAQGFSVTGVDPSPIAIER----------------ALLN 63

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034613500 111 VKFAWHketsseyqSRMLEKKELQKWDFIHMIQVNENL 148
Cdd:pfam13489  64 VRFDQF--------DEQEAAVPAGKFDVIVAREVLEHV 93
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 32-148 4.20e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.43  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613500  32 MQEFMDKKLPGIIGRIGDT-KSEIKILSIGGGAGeIDLQILSKVQAQYPGVCINNEVVEPsaeqiakykelvaktsNLEN 110
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKlPSPGRVLDFGCGTG-IFLRLLRAQGFSVTGVDPSPIAIER----------------ALLN 63

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034613500 111 VKFAWHketsseyqSRMLEKKELQKWDFIHMIQVNENL 148
Cdd:pfam13489  64 VRFDQF--------DEQEAAVPAGKFDVIVAREVLEHV 93
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 32-148 4.20e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.43  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613500  32 MQEFMDKKLPGIIGRIGDT-KSEIKILSIGGGAGeIDLQILSKVQAQYPGVCINNEVVEPsaeqiakykelvaktsNLEN 110
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKlPSPGRVLDFGCGTG-IFLRLLRAQGFSVTGVDPSPIAIER----------------ALLN 63

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034613500 111 VKFAWHketsseyqSRMLEKKELQKWDFIHMIQVNENL 148
Cdd:pfam13489  64 VRFDQF--------DEQEAAVPAGKFDVIVAREVLEHV 93
 
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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