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Conserved domains on  [gi|2572937377|ref|WP_308205983|]
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methyltransferase [Mycobacterium intermedium]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 108136)

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
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
125-332 6.22e-40

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 pfam00891:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 208  Bit Score: 139.85  E-value: 6.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572937377 125 WSMLAESVRTGRASIPRLRGKEFFAYLEDDPYLAELFNGAMTSISEMAELPVVAAYDFTPYRMIMDVGGGHGRLLAAILT 204
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQAIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572937377 205 AVPAARGVLFEIPDVVPGAQSLLrKLGVAERIQIETGSFFDGVPAGADLYFLKHIIHDWPDDQAVTILRNVRAAGGADAR 284
Cdd:pfam00891  81 LYPGCKGIVFDLPHVVEAAPTHF-SAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2572937377 285 VVLAELVIP-DHDRDFVGKWADLEMLLGLDGsRERTEDEYGTLLATAGF 332
Cdd:pfam00891 160 VILVESLLGaDPSGPLHTQLYSLNMLAQTEG-RERTEAEYSELLTGAGF 207
dimerization2 super family cl06920
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
26-100 2.24e-12

dimerization domain; This domain, found in methyltransferases, functions as a dimerization domain.


The actual alignment was detected with superfamily member pfam16864:

Pssm-ID: 471544  Cd Length: 87  Bit Score: 62.19  E-value: 2.24e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2572937377  26 VELILAGWTSQAIEAAAELGVADALVAGPMQPDDLAAKIGADPDAPSRLLRALCSRGVFRRRTD---GSYALTPLAAT 100
Cdd:pfam16864   2 LDLIDGFRASKVLFTACELGVFDLLAEGPLSAEEVAARLGASVDGTERLLDACVALGLLEREKTdgkGLYSNTELAST 79
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
125-332 6.22e-40

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 139.85  E-value: 6.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572937377 125 WSMLAESVRTGRASIPRLRGKEFFAYLEDDPYLAELFNGAMTSISEMAELPVVAAYDFTPYRMIMDVGGGHGRLLAAILT 204
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQAIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572937377 205 AVPAARGVLFEIPDVVPGAQSLLrKLGVAERIQIETGSFFDGVPAGADLYFLKHIIHDWPDDQAVTILRNVRAAGGADAR 284
Cdd:pfam00891  81 LYPGCKGIVFDLPHVVEAAPTHF-SAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2572937377 285 VVLAELVIP-DHDRDFVGKWADLEMLLGLDGsRERTEDEYGTLLATAGF 332
Cdd:pfam00891 160 VILVESLLGaDPSGPLHTQLYSLNMLAQTEG-RERTEAEYSELLTGAGF 207
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
26-100 2.24e-12

dimerization domain; This domain, found in methyltransferases, functions as a dimerization domain.


Pssm-ID: 465287  Cd Length: 87  Bit Score: 62.19  E-value: 2.24e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2572937377  26 VELILAGWTSQAIEAAAELGVADALVAGPMQPDDLAAKIGADPDAPSRLLRALCSRGVFRRRTD---GSYALTPLAAT 100
Cdd:pfam16864   2 LDLIDGFRASKVLFTACELGVFDLLAEGPLSAEEVAARLGASVDGTERLLDACVALGLLEREKTdgkGLYSNTELAST 79
 
Name Accession Description Interval E-value
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
125-332 6.22e-40

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 139.85  E-value: 6.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572937377 125 WSMLAESVRTGRASIPRLRGKEFFAYLEDDPYLAELFNGAMTSISEMAELPVVAAYDFTPYRMIMDVGGGHGRLLAAILT 204
Cdd:pfam00891   1 WRYLADAVREGRNQYNKAFGISLFEAIYRDEEERLLFNRGLQEHWSLIGKDVLTAFDLSGFRSLVDVGGGTGALAQAIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572937377 205 AVPAARGVLFEIPDVVPGAQSLLrKLGVAERIQIETGSFFDGVPAGADLYFLKHIIHDWPDDQAVTILRNVRAAGGADAR 284
Cdd:pfam00891  81 LYPGCKGIVFDLPHVVEAAPTHF-SAGEEPRVTFHGGDFFKDSLPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2572937377 285 VVLAELVIP-DHDRDFVGKWADLEMLLGLDGsRERTEDEYGTLLATAGF 332
Cdd:pfam00891 160 VILVESLLGaDPSGPLHTQLYSLNMLAQTEG-RERTEAEYSELLTGAGF 207
dimerization2 pfam16864
dimerization domain; This domain, found in methyltransferases, functions as a dimerization ...
26-100 2.24e-12

dimerization domain; This domain, found in methyltransferases, functions as a dimerization domain.


Pssm-ID: 465287  Cd Length: 87  Bit Score: 62.19  E-value: 2.24e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2572937377  26 VELILAGWTSQAIEAAAELGVADALVAGPMQPDDLAAKIGADPDAPSRLLRALCSRGVFRRRTD---GSYALTPLAAT 100
Cdd:pfam16864   2 LDLIDGFRASKVLFTACELGVFDLLAEGPLSAEEVAARLGASVDGTERLLDACVALGLLEREKTdgkGLYSNTELAST 79
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
189-278 5.55e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.89  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572937377 189 MDVGGGHGRLLAAILTAVPAARGVLFEI-PDVVPGAQSLLRKLG--VAERIQIETGSFFDGVPAGADLYFLKHIIHDWPD 265
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDIsPAALEAARERLAALGllNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80
                          90
                  ....*....|...
gi 2572937377 266 DQAVtiLRNVRAA 278
Cdd:pfam08242  81 PRAV--LRNIRRL 91
 
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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