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Conserved domains on  [gi|29244322|ref|NP_808461|]
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probable methyltransferase-like protein 24 precursor [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; ...
 170-295 6.79e-06

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 pfam13383:

Pssm-ID: 473071  Cd Length: 252  Bit Score: 46.95  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244322   170 HQIRSKR--CRLYSLGlGSDDTHFEVSM----ANGGCEVHRFDPSVKSAHVLERQGLWHHRLSIDWRDPHPAVAAQKPHG 243
Cdd:pfam13383  79 HRLIKHEidCLVYSVG-SNGDYQFEDGLidllGSDHCEIHVFDFGNFARSVNKEKNIHYHQWGLGSSYDNVYNPTMGNKG 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 29244322   244 NTRKLGSILNEFGH--HKIDVLKADLESAEWKVLENLILEDvleqIGQLVFEIH 295
Cdd:pfam13383 158 EILTFQDTQKLLGHklRTIDVFKIDCEKCEWENYKDWVAVD----IRQILVEVH 207
 
Name Accession Description Interval E-value
Methyltransf_22 pfam13383
Methyltransferase domain; This family appears to be a methyltransferase domain.
 170-295 6.79e-06

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


Pssm-ID: 372586  Cd Length: 252  Bit Score: 46.95  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244322   170 HQIRSKR--CRLYSLGlGSDDTHFEVSM----ANGGCEVHRFDPSVKSAHVLERQGLWHHRLSIDWRDPHPAVAAQKPHG 243
Cdd:pfam13383  79 HRLIKHEidCLVYSVG-SNGDYQFEDGLidllGSDHCEIHVFDFGNFARSVNKEKNIHYHQWGLGSSYDNVYNPTMGNKG 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 29244322   244 NTRKLGSILNEFGH--HKIDVLKADLESAEWKVLENLILEDvleqIGQLVFEIH 295
Cdd:pfam13383 158 EILTFQDTQKLLGHklRTIDVFKIDCEKCEWENYKDWVAVD----IRQILVEVH 207
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 178-295 1.53e-05

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 44.22  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244322   178 RLYSLGLGSDDTHFEVSMANGGCEVHRFDPSVKSAHVLERQglwhhrlsidwrdphpaVAaqkphgnTRKLGSILNEFGH 257
Cdd:TIGR01444  51 VLLNAAVGDRDGELEFNVSDDDTGNSSLLPTPDADRESEIE-----------------VE-------VVTLDDLVEEFGL 106

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 29244322   258 HKIDVLKADLESAEWKVLENLIlEDVLEQIGQLVFEIH 295
Cdd:TIGR01444 107 DKVDLLKIDVEGAELEVLRGAA-ETLLEKRPVIVLEVH 143
 
Name Accession Description Interval E-value
Methyltransf_22 pfam13383
Methyltransferase domain; This family appears to be a methyltransferase domain.
 170-295 6.79e-06

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


Pssm-ID: 372586  Cd Length: 252  Bit Score: 46.95  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244322   170 HQIRSKR--CRLYSLGlGSDDTHFEVSM----ANGGCEVHRFDPSVKSAHVLERQGLWHHRLSIDWRDPHPAVAAQKPHG 243
Cdd:pfam13383  79 HRLIKHEidCLVYSVG-SNGDYQFEDGLidllGSDHCEIHVFDFGNFARSVNKEKNIHYHQWGLGSSYDNVYNPTMGNKG 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 29244322   244 NTRKLGSILNEFGH--HKIDVLKADLESAEWKVLENLILEDvleqIGQLVFEIH 295
Cdd:pfam13383 158 EILTFQDTQKLLGHklRTIDVFKIDCEKCEWENYKDWVAVD----IRQILVEVH 207
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 178-295 1.53e-05

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 44.22  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244322   178 RLYSLGLGSDDTHFEVSMANGGCEVHRFDPSVKSAHVLERQglwhhrlsidwrdphpaVAaqkphgnTRKLGSILNEFGH 257
Cdd:TIGR01444  51 VLLNAAVGDRDGELEFNVSDDDTGNSSLLPTPDADRESEIE-----------------VE-------VVTLDDLVEEFGL 106

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 29244322   258 HKIDVLKADLESAEWKVLENLIlEDVLEQIGQLVFEIH 295
Cdd:TIGR01444 107 DKVDLLKIDVEGAELEVLRGAA-ETLLEKRPVIVLEVH 143
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 173-328 4.13e-04

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 40.63  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244322   173 RSKRCRLYSLGLGSDDThfEVSMANGGCEVHRFDPSvksaHVLERQGLWHHRLSIDWRDPHPAVaaqkphgNTRKLGSIL 252
Cdd:pfam05050  37 EKLDCTLLNLALGNDVG--LYEFYLGGKGGGGYLLF----AVGDPQGASTSSVLGGEEAKYIEV-------ETVTLDSFL 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29244322   253 NEFGHHKIDVLKADLESAEWKVLENliLEDVLE--QIGQLVFEIHLHWPGFEVSGSEsgvvrfwysLLKELERKHFRL 328
Cdd:pfam05050 104 EEIKKSDIDLLKIDVEGAELEVLEG--AEKTLKrcQPNIIVIEVHFFHYFGGPLFDE---------IRQFLRECGYRL 170
 
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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