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Conserved domains on  [gi|186507884|ref|NP_001118521|]
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S-adenosyl-L-methionine-dependent methyltransferases superfamily protein [Arabidopsis thaliana]

Protein Classification

TPMT family class I SAM-dependent methyltransferase( domain architecture ID 10529754)

TPMT family 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; similar to thiopurine S-methyltransferase (TPMT) that catalyzes the S-methylation of thiopurine drugs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 31-183 8.27e-79

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


:

Pssm-ID: 399030  Cd Length: 218  Bit Score: 234.63  E-value: 8.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   31 VAEGGWDKCWEDGVTPWDQGRATPLILHLLDSSALPLG-RTLVPGCGGGHDVVAMASPERFVVGLDISDKALNKANETYG 109
Cdd:pfam05724   1 VDPDFWLKRWVEGQTPFHQEGVNPLLVRHWDALKLPPGlRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVEKFFAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  110 SSPKAEYFSFVKE-----------DVFTWRPNEL--FDLIFDYVFFCAIEPEMRPAWGKSMHELLKPDGE--LITLMYPM 174
Cdd:pfam05724  81 LSPPITELSGFKEyssgnislycgDFFTLPREELgkFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRglLITLDYPQ 160


                  ....*....
gi 186507884  175 TDHEGGAPY 183
Cdd:pfam05724 161 TDHEGPPFS 169
 
Name Accession Description Interval E-value
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 31-183 8.27e-79

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 234.63  E-value: 8.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   31 VAEGGWDKCWEDGVTPWDQGRATPLILHLLDSSALPLG-RTLVPGCGGGHDVVAMASPERFVVGLDISDKALNKANETYG 109
Cdd:pfam05724   1 VDPDFWLKRWVEGQTPFHQEGVNPLLVRHWDALKLPPGlRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVEKFFAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  110 SSPKAEYFSFVKE-----------DVFTWRPNEL--FDLIFDYVFFCAIEPEMRPAWGKSMHELLKPDGE--LITLMYPM 174
Cdd:pfam05724  81 LSPPITELSGFKEyssgnislycgDFFTLPREELgkFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRglLITLDYPQ 160


                  ....*....
gi 186507884  175 TDHEGGAPY 183
Cdd:pfam05724 161 TDHEGPPFS 169
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 46-175 1.92e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.01  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  46 PWDQG---RATPLILHLLDSSA-LPLGRTLVP-GCGGGHDVVAMASPERF-VVGLDISDKALNKANETYGSSPKAEYfSF 119
Cdd:COG0500    1 PWDSYysdELLPGLAALLALLErLPKGGRVLDlGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAAKAGLGNV-EF 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 186507884 120 VKEDVFTWRPNEL--FDLIFDYVFFCAIEPEMRPAWGKSMHELLKPDGELITLMYPMT 175
Cdd:COG0500   80 LVADLAELDPLPAesFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAA 137
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-169 3.91e-08

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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 49.35  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  71 LVPGCGGGHDVVAMAS-PERFVVGLDISDKALNKAnETYGSSPKAEYFSFVKEDVFTWRPNEL--FDLIF-DYVFFCaiE 146
Cdd:cd02440    3 LDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADesFDVIIsDPPLHH--L 79

                         90       100
                 ....*....|....*....|...
gi 186507884 147 PEMRPAWGKSMHELLKPDGELIT 169
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
 74-170 3.25e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 43.00  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  74 GCGGGHDVVAMA---SPERFVVGLDISDKALNKANE-TYGSSPKAEYFSFVKEDV-FtwrPNELFDLIF-DYVFFCAIEP 147
Cdd:PRK08317  27 GCGPGNDARELArrvGPEGRVVGIDRSEAMLALAKErAAGLGPNVEFVRGDADGLpF---PDGSFDAVRsDRVLQHLEDP 103

                         90       100
                 ....*....|....*....|....*.
gi 186507884 148 EmrpawgKSMHEL---LKPDGELITL 170
Cdd:PRK08317 104 A------RALAEIarvLRPGGRVVVL 123
 
Name Accession Description Interval E-value
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 31-183 8.27e-79

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 234.63  E-value: 8.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   31 VAEGGWDKCWEDGVTPWDQGRATPLILHLLDSSALPLG-RTLVPGCGGGHDVVAMASPERFVVGLDISDKALNKANETYG 109
Cdd:pfam05724   1 VDPDFWLKRWVEGQTPFHQEGVNPLLVRHWDALKLPPGlRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVEKFFAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  110 SSPKAEYFSFVKE-----------DVFTWRPNEL--FDLIFDYVFFCAIEPEMRPAWGKSMHELLKPDGE--LITLMYPM 174
Cdd:pfam05724  81 LSPPITELSGFKEyssgnislycgDFFTLPREELgkFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRglLITLDYPQ 160


                  ....*....
gi 186507884  175 TDHEGGAPY 183
Cdd:pfam05724 161 TDHEGPPFS 169
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 46-175 1.92e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.01  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  46 PWDQG---RATPLILHLLDSSA-LPLGRTLVP-GCGGGHDVVAMASPERF-VVGLDISDKALNKANETYGSSPKAEYfSF 119
Cdd:COG0500    1 PWDSYysdELLPGLAALLALLErLPKGGRVLDlGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAAKAGLGNV-EF 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 186507884 120 VKEDVFTWRPNEL--FDLIFDYVFFCAIEPEMRPAWGKSMHELLKPDGELITLMYPMT 175
Cdd:COG0500   80 LVADLAELDPLPAesFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAA 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-165 4.22e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   74 GCGGGHDVVAMAspERF---VVGLDISDKALNKANETYGSS-PKAEyfsFVKEDVFTWR-PNELFDLIFDYVFFCAIEPE 148
Cdd:pfam13649   5 GCGTGRLTLALA--RRGgarVTGVDLSPEMLERARERAAEAgLNVE---FVQGDAEDLPfPDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 186507884  149 MRPAWGKSMHELLKPDG 165
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-168 1.48e-11

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 59.94  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  40 WEDGVTPWDQG--RATPLILHLLDSSalPLGRTLVPGCGGGHDVVAMAspERF---VVGLDISDKALNKANET---YGSS 111
Cdd:COG2230   25 FEDPDDTLEEAqeAKLDLILRKLGLK--PGMRVLDIGCGWGGLALYLA--RRYgvrVTGVTLSPEQLEYARERaaeAGLA 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 186507884 112 PKAEyfsFVKEDVFTWRPNELFDLIFDYVFFCAIEPEMRPAWGKSMHELLKPDGELI 168
Cdd:COG2230  101 DRVE---VRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 45-168 1.18e-10

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 56.56  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  45 TPWDqgratPLILHLLDSSALPLGRTLVPGCGGGHDVVAMAspERF--VVGLDISDKALNKANETYGSSPkaeyFSFVKE 122
Cdd:COG2227    8 DFWD-----RRLAALLARLLPAGGRVLDVGCGTGRLALALA--RRGadVTGVDISPEALEIARERAAELN----VDFVQG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 186507884 123 DVFTW-RPNELFDLIfdyVFFCAIE--PEMRPAWgKSMHELLKPDGELI 168
Cdd:COG2227   77 DLEDLpLEDGSFDLV---ICSEVLEhlPDPAALL-RELARLLKPGGLLL 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
74-168 4.23e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 54.44  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  74 GCGGGHDVVAMAS--PERFVVGLDISDKALNKANETYgssPKAEyfsFVKEDVFTWRPNELFDLIFD-YVFFCAiePEMR 150
Cdd:COG4106    9 GCGTGRLTALLAErfPGARVTGVDLSPEMLARARARL---PNVR---FVVADLRDLDPPEPFDLVVSnAALHWL--PDHA 80

                         90
                 ....*....|....*...
gi 186507884 151 PAWGKsMHELLKPDGELI 168
Cdd:COG4106   81 ALLAR-LAAALAPGGVLA 97
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 74-167 1.93e-08

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 50.06  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   74 GCGGGHDV--VAMASPERFVVGLDISDKALNKANETYGSspkAEYFSFVKEDVFTWRPNELFDLIFDYVF-FCAIE--PE 148
Cdd:pfam08242   4 GCGTGTLLraLLEALPGLEYTGLDISPAALEAARERLAA---LGLLNAVRVELFQLDLGELDPGSFDVVVaSNVLHhlAD 80

                          90
                  ....*....|....*....
gi 186507884  149 MRPAWgKSMHELLKPDGEL 167
Cdd:pfam08242  81 PRAVL-RNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-169 3.91e-08

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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 49.35  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  71 LVPGCGGGHDVVAMAS-PERFVVGLDISDKALNKAnETYGSSPKAEYFSFVKEDVFTWRPNEL--FDLIF-DYVFFCaiE 146
Cdd:cd02440    3 LDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADesFDVIIsDPPLHH--L 79

                         90       100
                 ....*....|....*....|...
gi 186507884 147 PEMRPAWGKSMHELLKPDGELIT 169
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 69-168 1.37e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.95  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   69 RTLVPGCGGGHDVVAMAS---PERFVVGLDISDKALNKANETyGSSPKAEYFSFVKEDVF---TWRPNELFDLIFDYVFF 142
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKAREN-AQKLGFDNVEFEQGDIEelpELLEDDKFDVVISNCVL 84

                          90       100
                  ....*....|....*....|....*.
gi 186507884  143 CAIePEMRPAWGKsMHELLKPDGELI 168
Cdd:pfam13847  85 NHI-PDPDKVLQE-ILRVLKPGGRLI 108
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 74-168 1.57e-07

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 47.66  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   74 GCGGGHDVVAMASPERFVVGLDISDKALNKANETYGSSPkaeyFSFVKEDV----FtwrPNELFDLIFDYVFFCAIEpEM 149
Cdd:pfam08241   4 GCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG----LTFVVGDAedlpF---PDNSFDLVLSSEVLHHVE-DP 75

                          90
                  ....*....|....*....
gi 186507884  150 RPAWgKSMHELLKPDGELI 168
Cdd:pfam08241  76 ERAL-REIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 74-194 2.92e-07

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 47.68  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  74 GCGGGHDVVAMASPERFVVGLDISDKALNKANETYGSSPKAeyFSFVKEDVFTWR-PNELFDLIFDYVFFCAIePEMRPA 152
Cdd:COG2226   30 GCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPfPDGSFDLVISSFVLHHL-PDPERA 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 186507884 153 WgKSMHELLKPDGELITLmypmtdhEGGAPYKVALSSYLRRC 194
Cdd:COG2226  107 L-AEIARVLKPGGRLVVV-------DFSPPDLAELEELLAEA 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
74-168 2.51e-06

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 45.76  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  74 GCGGGHDVVAMASPERFVVGLDISDKALNKANEtygsspKAEYFSFVKEDVFTWR-PNELFDLI-----FDYVffcaieP 147
Cdd:COG4976   54 GCGTGLLGEALRPRGYRLTGVDLSEEMLAKARE------KGVYDRLLVADLADLAePDGRFDLIvaadvLTYL------G 121

                         90       100
                 ....*....|....*....|.
gi 186507884 148 EMRPAWGKsMHELLKPDGELI 168
Cdd:COG4976  122 DLAAVFAG-VARALKPGGLFI 141
PRK08317 PRK08317
hypothetical protein; Provisional
 74-170 3.25e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 43.00  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884  74 GCGGGHDVVAMA---SPERFVVGLDISDKALNKANE-TYGSSPKAEYFSFVKEDV-FtwrPNELFDLIF-DYVFFCAIEP 147
Cdd:PRK08317  27 GCGPGNDARELArrvGPEGRVVGIDRSEAMLALAKErAAGLGPNVEFVRGDADGLpF---PDGSFDAVRsDRVLQHLEDP 103

                         90       100
                 ....*....|....*....|....*.
gi 186507884 148 EmrpawgKSMHEL---LKPDGELITL 170
Cdd:PRK08317 104 A------RALAEIarvLRPGGRVVVL 123
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-178 5.63e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 35.87  E-value: 5.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186507884   74 GCGGGHDVVAMAsPERF-VVGLDISDKALNKANetygssPKAEYFSFVKEDvfTWRPNELFDLIfdyVFFCAIE----Pe 148
Cdd:pfam13489  30 GCGTGIFLRLLR-AQGFsVTGVDPSPIAIERAL------LNVRFDQFDEQE--AAVPAGKFDVI---VAREVLEhvpdP- 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 186507884  149 mrPAWGKSMHELLKPDGeLITLMYPMTDHE 178
Cdd:pfam13489  97 --PALLRQIAALLKPGG-LLLLSTPLASDE 123
 
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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