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Conserved domains on  [gi|1677502157|ref|NP_077014|]
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methyltransferase-like protein 22 [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; ...
 164-337 5.24e-13

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: 66.59  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502157 164 SPHDIIRIEHTMatpLEDVGKQVWRGALLLADYIL------FRQDLFRGCTALELGAGTGLASIIAATMA--RTVYCTDV 235
Cdd:pfam10294   2 LDNPGLRIEEDT---GNGIGGHVWDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAVALLLpgASVTITDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502157 236 gADLLSMCQRNIALNSHlaatgGGIVRVKELDW---LKDDLCtDPKVPfswsqeeisDLydhttILfAAEVFYDDDLTDA 312
Cdd:pfam10294  79 -EEALELLKKNIELNAL-----SSKVVVKVLDWgenLPPDLF-DGHPV---------DL-----IL-AADCVYNEDSFPL 136

                         170       180
                  ....*....|....*....|....*
gi 1677502157 313 VFKTLSRLahrLKNACTAILSVEKR 337
Cdd:pfam10294 137 LEKTLKDL---LGKESVILVAYKKR 158
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 164-337 5.24e-13

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: 66.59  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502157 164 SPHDIIRIEHTMatpLEDVGKQVWRGALLLADYIL------FRQDLFRGCTALELGAGTGLASIIAATMA--RTVYCTDV 235
Cdd:pfam10294   2 LDNPGLRIEEDT---GNGIGGHVWDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAVALLLpgASVTITDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502157 236 gADLLSMCQRNIALNSHlaatgGGIVRVKELDW---LKDDLCtDPKVPfswsqeeisDLydhttILfAAEVFYDDDLTDA 312
Cdd:pfam10294  79 -EEALELLKKNIELNAL-----SSKVVVKVLDWgenLPPDLF-DGHPV---------DL-----IL-AADCVYNEDSFPL 136

                         170       180
                  ....*....|....*....|....*
gi 1677502157 313 VFKTLSRLahrLKNACTAILSVEKR 337
Cdd:pfam10294 137 LEKTLKDL---LGKESVILVAYKKR 158
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 190-250 1.01e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 43.59  E-value: 1.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677502157 190 ALLLADYILFRQdlfrGCTALELGAGTGLASIIAA--TMARTVYCTDVGADLLSMCQRNIALN 250
Cdd:COG4123    26 AVLLAAFAPVKK----GGRVLDLGTGTGVIALMLAqrSPGARITGVEIQPEAAELARRNVALN 84
PRK14968 PRK14968
putative methyltransferase; Provisional
 192-262 9.36e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.88  E-value: 9.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677502157 192 LLADYILFRQdlfrGCTALELGAGTGLASIIAATMARTVYCTDVGADLLSMCQRNIALNsHLAATGGGIVR 262
Cdd:PRK14968   14 LLAENAVDKK----GDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLN-NIRNNGVEVIR 79
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 164-337 5.24e-13

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: 66.59  E-value: 5.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502157 164 SPHDIIRIEHTMatpLEDVGKQVWRGALLLADYIL------FRQDLFRGCTALELGAGTGLASIIAATMA--RTVYCTDV 235
Cdd:pfam10294   2 LDNPGLRIEEDT---GNGIGGHVWDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAVALLLpgASVTITDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502157 236 gADLLSMCQRNIALNSHlaatgGGIVRVKELDW---LKDDLCtDPKVPfswsqeeisDLydhttILfAAEVFYDDDLTDA 312
Cdd:pfam10294  79 -EEALELLKKNIELNAL-----SSKVVVKVLDWgenLPPDLF-DGHPV---------DL-----IL-AADCVYNEDSFPL 136

                         170       180
                  ....*....|....*....|....*
gi 1677502157 313 VFKTLSRLahrLKNACTAILSVEKR 337
Cdd:pfam10294 137 LEKTLKDL---LGKESVILVAYKKR 158
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 190-250 1.01e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 43.59  E-value: 1.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677502157 190 ALLLADYILFRQdlfrGCTALELGAGTGLASIIAA--TMARTVYCTDVGADLLSMCQRNIALN 250
Cdd:COG4123    26 AVLLAAFAPVKK----GGRVLDLGTGTGVIALMLAqrSPGARITGVEIQPEAAELARRNVALN 84
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
210-250 3.39e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 41.95  E-value: 3.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1677502157 210 LELGAGTGLASIIAA-TMARTVYCTDVGADLLSMCQRNIALN 250
Cdd:COG4076    40 LDIGTGSGLLSMLAArAGAKKVYAVEVNPDIAAVARRIIAAN 81
PRK14968 PRK14968
putative methyltransferase; Provisional
 192-262 9.36e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.88  E-value: 9.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677502157 192 LLADYILFRQdlfrGCTALELGAGTGLASIIAATMARTVYCTDVGADLLSMCQRNIALNsHLAATGGGIVR 262
Cdd:PRK14968   14 LLAENAVDKK----GDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLN-NIRNNGVEVIR 79
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 192-281 6.24e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.59  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502157 192 LLADYILFRQDLFRGCTALELGAGTG-LASIIAATMARTVYCTDVGADLLSMCQRNialnshLAATGGGIVRVKELDWLK 270
Cdd:COG0500    13 GLAALLALLERLPKGGRVLDLGCGTGrNLLALAARFGGRVIGIDLSPEAIALARAR------AAKAGLGNVEFLVADLAE 86

                          90
                  ....*....|.
gi 1677502157 271 DDLCTDPKVPF 281
Cdd:COG0500    87 LDPLPAESFDL 97
 
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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