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Conserved domains on  [gi|1266290644|gb|PHB81934|]
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class I SAM-dependent methyltransferase [Bacillus toyonensis]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10552639)

class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_14 pfam08484
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase ...
242-400 2.76e-82

C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase proteins. This domain is found C-terminal to methyltransferase domains such as pfam08241 or pfam08242. But this domain is not a methyltransferase.


:

Pssm-ID: 430022  Cd Length: 160  Bit Score: 248.91  E-value: 2.76e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 242 STHGGSLRIFIKHLSAQS-TIHSNVTNLIQKEIDHGLDTLDCYLLFSKRVEQLKINILKFFIEAKALNKQIIGYGAPAKG 320
Cdd:pfam08484   1 PTHGGSLRVYAARKEGGArPVSPAVAALLAEERAAGLDTLATYAGFAERVERVKDELLALLIDLKAEGKRVAGYGAAAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 321 NTLLNYCGIGKEFLAYTVDKNPHKQNLLLPGTRIPIKSPEEIKRTKPDYILILPWNLKDEIMKECSFIREWGGKFLVTVP 400
Cdd:pfam08484  81 NTLLNYCGIGPDLLDYVVDRNPAKQGRYTPGTHIPIVPPEKLREDRPDYVLILPWNLADEIMAQLAEYREWGGKFIVPVP 160
Methyltransf_13 pfam08421
Putative zinc binding domain; This domain is found at the N-terminus of bacterial ...
6-67 4.68e-26

Putative zinc binding domain; This domain is found at the N-terminus of bacterial methyltransferases and contains four conserved cysteines suggesting a potential zinc binding domain.


:

Pssm-ID: 429987  Cd Length: 62  Bit Score: 99.58  E-value: 4.68e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266290644   6 CRFCHSLLTNSFLDLGVSPLANSFIAPKNSYKMEPFYPLHTFVCNSCLLVQLDEFESPNNIF 67
Cdd:pfam08421   1 CRLCGSPLLTPFLDLGRQPLANAFLTPEQLDQPEPFYPLRLVVCEDCGLVQLEEVVPPEELF 62
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
96-198 1.39e-17

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: 78.52  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  96 HLTKNSQVIEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKGIPTEVNFFSNDLANnLP----QADLIIANNVLAH 171
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDLED-LPledgSFDLVICSEVLEH 99
                          90       100
                  ....*....|....*....|....*..
gi 1266290644 172 VPNLHDFVAGLKTLLKRDGTITIEFPH 198
Cdd:COG2227   100 LPDPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
Methyltransf_14 pfam08484
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase ...
242-400 2.76e-82

C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase proteins. This domain is found C-terminal to methyltransferase domains such as pfam08241 or pfam08242. But this domain is not a methyltransferase.


Pssm-ID: 430022  Cd Length: 160  Bit Score: 248.91  E-value: 2.76e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 242 STHGGSLRIFIKHLSAQS-TIHSNVTNLIQKEIDHGLDTLDCYLLFSKRVEQLKINILKFFIEAKALNKQIIGYGAPAKG 320
Cdd:pfam08484   1 PTHGGSLRVYAARKEGGArPVSPAVAALLAEERAAGLDTLATYAGFAERVERVKDELLALLIDLKAEGKRVAGYGAAAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 321 NTLLNYCGIGKEFLAYTVDKNPHKQNLLLPGTRIPIKSPEEIKRTKPDYILILPWNLKDEIMKECSFIREWGGKFLVTVP 400
Cdd:pfam08484  81 NTLLNYCGIGPDLLDYVVDRNPAKQGRYTPGTHIPIVPPEKLREDRPDYVLILPWNLADEIMAQLAEYREWGGKFIVPVP 160
Methyltransf_13 pfam08421
Putative zinc binding domain; This domain is found at the N-terminus of bacterial ...
6-67 4.68e-26

Putative zinc binding domain; This domain is found at the N-terminus of bacterial methyltransferases and contains four conserved cysteines suggesting a potential zinc binding domain.


Pssm-ID: 429987  Cd Length: 62  Bit Score: 99.58  E-value: 4.68e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266290644   6 CRFCHSLLTNSFLDLGVSPLANSFIAPKNSYKMEPFYPLHTFVCNSCLLVQLDEFESPNNIF 67
Cdd:pfam08421   1 CRLCGSPLLTPFLDLGRQPLANAFLTPEQLDQPEPFYPLRLVVCEDCGLVQLEEVVPPEELF 62
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
96-198 1.39e-17

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: 78.52  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  96 HLTKNSQVIEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKGIPTEVNFFSNDLANnLP----QADLIIANNVLAH 171
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDLED-LPledgSFDLVICSEVLEH 99
                          90       100
                  ....*....|....*....|....*..
gi 1266290644 172 VPNLHDFVAGLKTLLKRDGTITIEFPH 198
Cdd:COG2227   100 LPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
97-236 4.80e-13

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 66.68  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  97 LTKNSQVIEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKGIPteVNFFSNDLANNLPQADLIIANNVLAHVPNLH 176
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRF--DQFDEQEAAVPAGKFDVIVAREVLEHVPDPP 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1266290644 177 DFVAGLKTLLKRDGTITIEFP----HLLNLISCKQFDTIYHEHFSYFSLISLQKILAHHHLQIV 236
Cdd:pfam13489  98 ALLRQIAALLKPGGLLLLSTPlasdEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGFEVV 161
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
103-199 1.13e-03

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: 38.18  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 103 VIEIASNDGYLLQYFLK-ENINTLGIEPAKNVAEIAIQK---GIPTEVNFFSNDLANNLPQA----DLIIANNVLAH-VP 173
Cdd:cd02440     2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAaaaLLADNVEVLKGDAEELPPEAdesfDVIISDPPLHHlVE 81
                          90       100
                  ....*....|....*....|....*.
gi 1266290644 174 NLHDFVAGLKTLLKRDGTITIEFPHL 199
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
Methyltransf_14 pfam08484
C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase ...
242-400 2.76e-82

C-methyltransferase C-terminal domain; This domain is found in bacterial C-methyltransferase proteins. This domain is found C-terminal to methyltransferase domains such as pfam08241 or pfam08242. But this domain is not a methyltransferase.


Pssm-ID: 430022  Cd Length: 160  Bit Score: 248.91  E-value: 2.76e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 242 STHGGSLRIFIKHLSAQS-TIHSNVTNLIQKEIDHGLDTLDCYLLFSKRVEQLKINILKFFIEAKALNKQIIGYGAPAKG 320
Cdd:pfam08484   1 PTHGGSLRVYAARKEGGArPVSPAVAALLAEERAAGLDTLATYAGFAERVERVKDELLALLIDLKAEGKRVAGYGAAAKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 321 NTLLNYCGIGKEFLAYTVDKNPHKQNLLLPGTRIPIKSPEEIKRTKPDYILILPWNLKDEIMKECSFIREWGGKFLVTVP 400
Cdd:pfam08484  81 NTLLNYCGIGPDLLDYVVDRNPAKQGRYTPGTHIPIVPPEKLREDRPDYVLILPWNLADEIMAQLAEYREWGGKFIVPVP 160
Methyltransf_13 pfam08421
Putative zinc binding domain; This domain is found at the N-terminus of bacterial ...
6-67 4.68e-26

Putative zinc binding domain; This domain is found at the N-terminus of bacterial methyltransferases and contains four conserved cysteines suggesting a potential zinc binding domain.


Pssm-ID: 429987  Cd Length: 62  Bit Score: 99.58  E-value: 4.68e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266290644   6 CRFCHSLLTNSFLDLGVSPLANSFIAPKNSYKMEPFYPLHTFVCNSCLLVQLDEFESPNNIF 67
Cdd:pfam08421   1 CRLCGSPLLTPFLDLGRQPLANAFLTPEQLDQPEPFYPLRLVVCEDCGLVQLEEVVPPEELF 62
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
96-198 1.39e-17

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: 78.52  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  96 HLTKNSQVIEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKGIPTEVNFFSNDLANnLP----QADLIIANNVLAH 171
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDLED-LPledgSFDLVICSEVLEH 99
                          90       100
                  ....*....|....*....|....*..
gi 1266290644 172 VPNLHDFVAGLKTLLKRDGTITIEFPH 198
Cdd:COG2227   100 LPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
97-236 4.80e-13

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 66.68  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  97 LTKNSQVIEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKGIPteVNFFSNDLANNLPQADLIIANNVLAHVPNLH 176
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRF--DQFDEQEAAVPAGKFDVIVAREVLEHVPDPP 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1266290644 177 DFVAGLKTLLKRDGTITIEFP----HLLNLISCKQFDTIYHEHFSYFSLISLQKILAHHHLQIV 236
Cdd:pfam13489  98 ALLRQIAALLKPGGLLLLSTPlasdEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGFEVV 161
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
85-235 6.22e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 66.56  E-value: 6.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  85 KQYVEMAIERFHLTKNSQVIEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKGIptEVNFFSNDLANnLPQ----A 160
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGV--YDRLLVADLAD-LAEpdgrF 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1266290644 161 DLIIANNVLAHVPNLHDFVAGLKTLLKRDGTITIEFPHLlnlisckqfdtiYHEHFSYFSLISLQKILAHHHLQI 235
Cdd:COG4976   109 DLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDA------------DGSGRYAHSLDYVRDLLAAAGFEV 171
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
104-192 4.66e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.22  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 104 IEIASNDGYLLQYFLKENINT--LGIEPAKNVAEIAIQK------GIPTEVNFFSNDLANNLP-QADLIIANNVLAHVPN 174
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARERlaalglLNAVRVELFQLDLGELDPgSFDVVVASNVLHHLAD 80
                          90
                  ....*....|....*...
gi 1266290644 175 LHDFVAGLKTLLKRDGTI 192
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
80-194 4.07e-09

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: 54.61  E-value: 4.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  80 WLQHAKQY--VEMAIERFHLTKNSQVIEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKG--IPTEVNFFSNDlAN 155
Cdd:COG2226     1 FDRVAARYdgREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAaeAGLNVEFVVGD-AE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1266290644 156 NLP----QADLIIANNVLAHVPNLHDFVAGLKTLLKRDGTITI 194
Cdd:COG2226    80 DLPfpdgSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
104-192 7.30e-08

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.97  E-value: 7.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 104 IEIASNDGYLLQYFLKENINTLGIEPAKNVAEIAIQKGIPTEVNFFSNDlANNLP----QADLIIANNVLAHVPNLHDFV 179
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGD-AEDLPfpdnSFDLVLSSEVLHHVEDPERAL 79
                          90
                  ....*....|...
gi 1266290644 180 AGLKTLLKRDGTI 192
Cdd:pfam08241  80 REIARVLKPGGIL 92
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
96-192 2.89e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.83  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  96 HLTKNSQVIEIASNDGYLLQYFLKEN--------INTLGIEPAKNVAEIAIQKGIPTEVNFFSNDLANNLPQADLIIANN 167
Cdd:COG0500    23 RLPKGGRVLDLGCGTGRNLLALAARFggrvigidLSPEAIALARARAAKAGLGNVEFLVADLAELDPLPAESFDLVVAFG 102
                          90       100
                  ....*....|....*....|....*..
gi 1266290644 168 VLAHVP--NLHDFVAGLKTLLKRDGTI 192
Cdd:COG0500   103 VLHHLPpeEREALLRELARALKPGGVL 129
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
99-196 2.89e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  99 KNSQVIEIASNDGYLLQYFLKENINT--LGIEPAKNVAEIAIQKGipTEVNFFSNDLANNLP--QADLIIANNVLAHVPN 174
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGArvTGVDLSPEMLARARARL--PNVRFVVADLRDLDPpePFDLVVSNAALHWLPD 78
                          90       100
                  ....*....|....*....|..
gi 1266290644 175 LHDFVAGLKTLLKRDGTITIEF 196
Cdd:COG4106    79 HAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
103-190 5.08e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.08  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 103 VIEIASNDGYLLQYFLKE-NINTLGIEPAKNVAEIAIQKGIPTEVNF-FSNDLANNLPQA----DLIIANNVLAHV--PN 174
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVeFVQGDAEDLPFPdgsfDLVVSSGVLHHLpdPD 80
                          90
                  ....*....|....*.
gi 1266290644 175 LHDFVAGLKTLLKRDG 190
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
103-199 1.13e-03

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: 38.18  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644 103 VIEIASNDGYLLQYFLK-ENINTLGIEPAKNVAEIAIQK---GIPTEVNFFSNDLANNLPQA----DLIIANNVLAH-VP 173
Cdd:cd02440     2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAaaaLLADNVEVLKGDAEELPPEAdesfDVIISDPPLHHlVE 81
                          90       100
                  ....*....|....*....|....*.
gi 1266290644 174 NLHDFVAGLKTLLKRDGTITIEFPHL 199
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVLTLVLA 107
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
97-201 7.64e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 36.63  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266290644  97 LTKNSQVIEIASNDGYLLqYFLKENINT----LGI---EPAKNVAEIAIQKGIPTEVNFFSNDlANNLPQA------DLI 163
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLS-FELAEELGPnaevVGIdisEEAIEKARENAQKLGFDNVEFEQGD-IEELPELleddkfDVV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1266290644 164 IANNVLAHVPNLHDFVAGLKTLLKRDGTITIEFPHLLN 201
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLA 116
 
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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