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Conserved domains on  [gi|1310926255|ref|WP_101052875|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Shewanella]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10606006)

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 histamine N-methyltransferase

CATH:  2.20.25.110
EC:  2.1.-.-|2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
PubMed:  12826405|12504684

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 65-197 2.76e-18

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


:

Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 78.24  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  65 FLQRLLTPAMTFLRPGMQGLDFGCGPGPTLsKLLAREGIACDDFDPLF------------------FPNPLQAQYDFILS 126
Cdd:pfam13489   8 LLADLLLRLLPKLPSPGRVLDFGCGTGIFL-RLLRAQGFSVTGVDPSPiaierallnvrfdqfdeqEAAVPAGKFDVIVA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310926255 127 SECFEHLHRPAAEISALLARLVPGGYLGIMT--DRWQSEAQFYDWHYTRDP-THCSFFHRATLDWLCETFALNL 197
Cdd:pfam13489  87 REVLEHVPDPPALLRQIAALLKPGGLLLLSTplASDEADRLLLEWPYLRPRnGHISLFSARSLKRLLEEAGFEV 160
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 65-197 2.76e-18

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 78.24  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  65 FLQRLLTPAMTFLRPGMQGLDFGCGPGPTLsKLLAREGIACDDFDPLF------------------FPNPLQAQYDFILS 126
Cdd:pfam13489   8 LLADLLLRLLPKLPSPGRVLDFGCGTGIFL-RLLRAQGFSVTGVDPSPiaierallnvrfdqfdeqEAAVPAGKFDVIVA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310926255 127 SECFEHLHRPAAEISALLARLVPGGYLGIMT--DRWQSEAQFYDWHYTRDP-THCSFFHRATLDWLCETFALNL 197
Cdd:pfam13489  87 REVLEHVPDPPALLRQIAALLKPGGLLLLSTplASDEADRLLLEWPYLRPRnGHISLFSARSLKRLLEEAGFEV 160
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 68-157 4.11e-12

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: 60.80  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  68 RLLTPAMTFLRPGMQGLDFGCGPGpTLSKLLAREG---IACD-----------------------DFDPLFFPNplqAQY 121
Cdd:COG2227    13 RLAALLARLLPAGGRVLDVGCGTG-RLALALARRGadvTGVDispealeiareraaelnvdfvqgDLEDLPLED---GSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1310926255 122 DFILSSECFEHLHRPAAEISALLARLVPGGYLGIMT 157
Cdd:COG2227    89 DLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
PRK08317 PRK08317
hypothetical protein; Provisional
 60-162 3.09e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 37.61  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  60 PGYVGFLQRLLtpAMTFLRPGMQGLDFGCGPGpTLSKLLARE--------GI-------------ACDDFDPLFFPN--- 115
Cdd:PRK08317    2 PDFRRYRARTF--ELLAVQPGDRVLDVGCGPG-NDARELARRvgpegrvvGIdrseamlalakerAAGLGPNVEFVRgda 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1310926255 116 ---PLQAQY-DFILSSECFEHLHRPAAEISALLARLVPGGYLGIMTDRWQS 162
Cdd:PRK08317   79 dglPFPDGSfDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWDT 129
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-153 6.08e-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: 35.10  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  84 LDFGCGPGPTLSKLLAREG------------------------------IACDDFDPLFFPNPlqaQYDFILSSECFEHL 133
Cdd:cd02440     3 LDLGCGTGALALALASGPGarvtgvdispvalelarkaaaalladnvevLKGDAEELPPEADE---SFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|.
gi 1310926255 134 H-RPAAEISALLARLVPGGYL 153
Cdd:cd02440    80 VeDLARFLEEARRLLKPGGVL 100
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 65-197 2.76e-18

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 78.24  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  65 FLQRLLTPAMTFLRPGMQGLDFGCGPGPTLsKLLAREGIACDDFDPLF------------------FPNPLQAQYDFILS 126
Cdd:pfam13489   8 LLADLLLRLLPKLPSPGRVLDFGCGTGIFL-RLLRAQGFSVTGVDPSPiaierallnvrfdqfdeqEAAVPAGKFDVIVA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310926255 127 SECFEHLHRPAAEISALLARLVPGGYLGIMT--DRWQSEAQFYDWHYTRDP-THCSFFHRATLDWLCETFALNL 197
Cdd:pfam13489  87 REVLEHVPDPPALLRQIAALLKPGGLLLLSTplASDEADRLLLEWPYLRPRnGHISLFSARSLKRLLEEAGFEV 160
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 68-157 4.11e-12

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: 60.80  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  68 RLLTPAMTFLRPGMQGLDFGCGPGpTLSKLLAREG---IACD-----------------------DFDPLFFPNplqAQY 121
Cdd:COG2227    13 RLAALLARLLPAGGRVLDVGCGTG-RLALALARRGadvTGVDispealeiareraaelnvdfvqgDLEDLPLED---GSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1310926255 122 DFILSSECFEHLHRPAAEISALLARLVPGGYLGIMT 157
Cdd:COG2227    89 DLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
84-153 1.75e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 50.21  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  84 LDFGCGPGpTLSKLLAREGIACD----DFDPLF-------FPN-----------PLQAQYDFILSSECFEHLHRPAAEIS 141
Cdd:COG4106     6 LDLGCGTG-RLTALLAERFPGARvtgvDLSPEMlarararLPNvrfvvadlrdlDPPEPFDLVVSNAALHWLPDHAALLA 84

                          90
                  ....*....|..
gi 1310926255 142 ALLARLVPGGYL 153
Cdd:COG4106    85 RLAAALAPGGVL 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 77-169 2.87e-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: 48.07  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  77 LRPGMQGLDFGCGPGPTLSKLLAREG--IACD-------------------------DFDPLFFPNplqAQYDFILSSEC 129
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAERGArvTGVDispemlelareraaeaglnvefvvgDAEDLPFPD---GSFDLVISSFV 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1310926255 130 FEHLHRPAAEISALLARLVPGGYLGIMTDRWQSEAQFYDW 169
Cdd:COG2226    97 LHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-151 3.65e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.09  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  84 LDFGCGPGpTLSKLLAREG----IACD-------------------------DFDPLFFPNplqAQYDFILSSECFEHLH 134
Cdd:pfam13649   2 LDLGCGTG-RLTLALARRGgarvTGVDlspemlerareraaeaglnvefvqgDAEDLPFPD---GSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 1310926255 135 RPAAE--ISALLARLVPGG 151
Cdd:pfam13649  78 DPDLEaaLREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 77-155 3.85e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.31  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  77 LRPGMQGLDFGCGPGP----------------TLSK--------LLAREGIACD------DFDPLffpnPLQAQYDFILS 126
Cdd:COG2230    49 LKPGMRVLDIGCGWGGlalylarrygvrvtgvTLSPeqleyareRAAEAGLADRvevrlaDYRDL----PADGQFDAIVS 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1310926255 127 SECFEHLHRPAAE--ISALLARLVPGGYLGI 155
Cdd:COG2230   125 IGMFEHVGPENYPayFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
50-167 3.02e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.06  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  50 YDTHEnsIDDPGYVGfLQRLLTPAMTFLRPGMQG--LDFGCGPGPTLSKLLAR----EGI-------------------A 104
Cdd:COG4976    18 YDAAL--VEDLGYEA-PALLAEELLARLPPGPFGrvLDLGCGTGLLGEALRPRgyrlTGVdlseemlakarekgvydrlL 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310926255 105 CDDFDPLFFPNplqAQYDFILSSECFEHLHRPAAEISALLARLVPGGYLGIMTDRWQSEAQFY 167
Cdd:COG4976    95 VADLADLAEPD---GRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADGSGRYA 154
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-155 8.87e-05

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: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  49 FYDTHENSIDDPGYVGFLQRLLTpamtfLRPGMQGLDFGCGPGPTLSKLLAREGIACD--DFDP---------------- 110
Cdd:COG0500     1 PWDSYYSDELLPGLAALLALLER-----LPKGGRVLDLGCGTGRNLLALAARFGGRVIgiDLSPeaialararaakaglg 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1310926255 111 --------LFFPNPL-QAQYDFILSSECFEHLhrPAAEISALLAR----LVPGGYLGI 155
Cdd:COG0500    76 nveflvadLAELDPLpAESFDLVVAFGVLHHL--PPEEREALLRElaraLKPGGVLLL 131
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-153 1.02e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.04  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  84 LDFGCGPGPTLSKLLA----------------------------REGIACDDFDPLFFPNPLQAQYDFILSSECFEHLHR 135
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalpgleytgldispaaleaarerlaalgLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1310926255 136 PAAEISALLARLVPGGYL 153
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-153 5.84e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  84 LDFGCGPGPtLSKLLAREG---IACD-----------------------DFDPLFFPNplqAQYDFILSSECFEHLHRPA 137
Cdd:pfam08241   1 LDVGCGTGL-LTELLARLGarvTGVDispemlelarekapregltfvvgDAEDLPFPD---NSFDLVLSSEVLHHVEDPE 76

                          90
                  ....*....|....*....
gi 1310926255 138 ---AEISALLArlvPGGYL 153
Cdd:pfam08241  77 ralREIARVLK---PGGIL 92
PRK08317 PRK08317
hypothetical protein; Provisional
 60-162 3.09e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 37.61  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  60 PGYVGFLQRLLtpAMTFLRPGMQGLDFGCGPGpTLSKLLARE--------GI-------------ACDDFDPLFFPN--- 115
Cdd:PRK08317    2 PDFRRYRARTF--ELLAVQPGDRVLDVGCGPG-NDARELARRvgpegrvvGIdrseamlalakerAAGLGPNVEFVRgda 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1310926255 116 ---PLQAQY-DFILSSECFEHLHRPAAEISALLARLVPGGYLGIMTDRWQS 162
Cdd:PRK08317   79 dglPFPDGSfDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWDT 129
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-153 6.08e-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: 35.10  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310926255  84 LDFGCGPGPTLSKLLAREG------------------------------IACDDFDPLFFPNPlqaQYDFILSSECFEHL 133
Cdd:cd02440     3 LDLGCGTGALALALASGPGarvtgvdispvalelarkaaaalladnvevLKGDAEELPPEADE---SFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|.
gi 1310926255 134 H-RPAAEISALLARLVPGGYL 153
Cdd:cd02440    80 VeDLARFLEEARRLLKPGGVL 100
 
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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