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Conserved domains on  [gi|1864203801|gb|QLC26646|]
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class I SAM-dependent methyltransferase [Parasphingopyxis algicola]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
135-246 5.71e-20

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: 84.30  E-value: 5.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 135 ARIRRYLGDdvHWGPGTRILEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYGRQR--WLNLRLETIDHLKLSFRP---D 209
Cdd:COG2227    12 RRLAALLAR--LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaELNVDFVQGDLEDLPLEDgsfD 89
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1864203801 210 LVIYRHVLEHLDNPIEELRKIAAICRRGtGMLYVEVP 246
Cdd:COG2227    90 LVICSEVLEHLPDPAALLRELARLLKPG-GLLLLSTP 125
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
135-246 5.71e-20

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: 84.30  E-value: 5.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 135 ARIRRYLGDdvHWGPGTRILEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYGRQR--WLNLRLETIDHLKLSFRP---D 209
Cdd:COG2227    12 RRLAALLAR--LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaELNVDFVQGDLEDLPLEDgsfD 89
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1864203801 210 LVIYRHVLEHLDNPIEELRKIAAICRRGtGMLYVEVP 246
Cdd:COG2227    90 LVICSEVLEHLPDPAALLRELARLLKPG-GLLLLSTP 125
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
126-288 1.14e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 62.06  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 126 FFRKQQRIGARIRRYLGDDvHWGPGtRILEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYGRQRWLNLRLETIDHLKLS 205
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPK-LPSPG-RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 206 FRPDLVIYRHVLEHLDNPIEELRKIAAICRRGtGMLYVEVPGVDSMSTAPTHVGGDLLktLQNAHNFYFSRKSLANVLTM 285
Cdd:pfam13489  79 GKFDVIVAREVLEHVPDPPALLRQIAALLKPG-GLLLLSTPLASDEADRLLLEWPYLR--PRNGHISLFSARSLKRLLEE 155

                  ...
gi 1864203801 286 SGF 288
Cdd:pfam13489 156 AGF 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
152-245 4.03e-07

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: 47.81  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 152 RILEVGTGAGG-TLEYLCRDGAIGLGLDLDASYLEYGRQRWLNLRLETIDHLKLSF---------RPDLVIYRHVLEHL- 220
Cdd:cd02440     1 RVLDLGCGTGAlALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAeelppeadeSFDVIISDPPLHHLv 80
                          90       100
                  ....*....|....*....|....*
gi 1864203801 221 DNPIEELRKIAAICRRGtGMLYVEV 245
Cdd:cd02440    81 EDLARFLEEARRLLKPG-GVLVLTL 104
PRK08317 PRK08317
hypothetical protein; Provisional
131-237 9.67e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.31  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 131 QRIGARIRRYLgddvHWGPGTRILEVGTGAGGTLEYLCRD-GAIG--LGLDLDASYLEYGRQRW----LNLRLETIDHLK 203
Cdd:PRK08317    5 RRYRARTFELL----AVQPGDRVLDVGCGPGNDARELARRvGPEGrvVGIDRSEAMLALAKERAaglgPNVEFVRGDADG 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1864203801 204 LSFRP---DLVIYRHVLEHLDNPIEELRKIAAICRRG 237
Cdd:PRK08317   81 LPFPDgsfDAVRSDRVLQHLEDPARALAEIARVLRPG 117
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
135-246 5.71e-20

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: 84.30  E-value: 5.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 135 ARIRRYLGDdvHWGPGTRILEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYGRQR--WLNLRLETIDHLKLSFRP---D 209
Cdd:COG2227    12 RRLAALLAR--LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaELNVDFVQGDLEDLPLEDgsfD 89
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1864203801 210 LVIYRHVLEHLDNPIEELRKIAAICRRGtGMLYVEVP 246
Cdd:COG2227    90 LVICSEVLEHLPDPAALLRELARLLKPG-GLLLLSTP 125
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
138-243 1.72e-15

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: 72.33  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 138 RRYLGDDVHWGPGTRILEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYGRQR----WLNLRLETIDHLKLSFRP---DL 210
Cdd:COG2226    11 REALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaeaGLNVEFVVGDAEDLPFPDgsfDL 90
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1864203801 211 VIYRHVLEHLDNPIEELRKIAAICRRGtGMLYV 243
Cdd:COG2226    91 VISSFVLHHLPDPERALAEIARVLKPG-GRLVV 122
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
126-288 1.14e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 62.06  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 126 FFRKQQRIGARIRRYLGDDvHWGPGtRILEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYGRQRWLNLRLETIDHLKLS 205
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPK-LPSPG-RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 206 FRPDLVIYRHVLEHLDNPIEELRKIAAICRRGtGMLYVEVPGVDSMSTAPTHVGGDLLktLQNAHNFYFSRKSLANVLTM 285
Cdd:pfam13489  79 GKFDVIVAREVLEHVPDPPALLRQIAALLKPG-GLLLLSTPLASDEADRLLLEWPYLR--PRNGHISLFSARSLKRLLEE 155

                  ...
gi 1864203801 286 SGF 288
Cdd:pfam13489 156 AGF 158
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
154-243 2.18e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.60  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 154 LEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYGRQR----WLNLRLETIDHLKL---SFrpDLVIYRHVLEHLDNPIEE 226
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKapreGLTFVVGDAEDLPFpdnSF--DLVLSSEVLHHVEDPERA 78
                          90
                  ....*....|....*..
gi 1864203801 227 LRKIAAICRRGtGMLYV 243
Cdd:pfam08241  79 LREIARVLKPG-GILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
149-245 2.83e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 59.45  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 149 PGTRILEVGTGAGGTLEYLCR--DGAIGLGLDLDASYLEYGRQRWLNLRLETID--HLKLSFRPDLVIYRHVLEHLDNPI 224
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAErfPGARVTGVDLSPEMLARARARLPNVRFVVADlrDLDPPEPFDLVVSNAALHWLPDHA 80
                          90       100
                  ....*....|....*....|.
gi 1864203801 225 EELRKIAAICRRGtGMLYVEV 245
Cdd:COG4106    81 ALLARLAAALAPG-GVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
153-237 2.11e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 54.11  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 153 ILEVGTGAGGTLEYLCRD-GAIGLGLDLDASYLEYGRQRW----LNLRLETIDHLKLSFRP---DLVIYRHVLEHLDNPI 224
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDgsfDLVVSSGVLHHLPDPD 80
                          90
                  ....*....|....*
gi 1864203801 225 EE--LRKIAAICRRG 237
Cdd:pfam13649  81 LEaaLREIARVLKPG 95
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
154-241 8.54e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 52.37  E-value: 8.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 154 LEVGTGAGGTLEYLCRDGAIG--LGLDLDASYLEYGRQR--------WLNLRLETIDHLKLSFRP-DLVIYRHVLEHLDN 222
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARERlaalgllnAVRVELFQLDLGELDPGSfDVVVASNVLHHLAD 80
                          90
                  ....*....|....*....
gi 1864203801 223 PIEELRKIAAICRRGtGML 241
Cdd:pfam08242  81 PRAVLRNIRRLLKPG-GVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
108-293 6.20e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.92  E-value: 6.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 108 YATLYrDLYVGRTLDlrefFRKQQRIGARIRRYLGDdvhwGPGTRILEVGTGAGGTLEYLCRDGAIGLGLDLDASYLEYG 187
Cdd:COG4976    14 YADSY-DAALVEDLG----YEAPALLAEELLARLPP----GPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 188 RQRWLNLRLETIDHLKLSFRP---DLVIYRHVLEHLDNPIEELRKIAAICRRGtGMLYVEVPgvdsmstapthvggdllk 264
Cdd:COG4976    85 REKGVYDRLLVADLADLAEPDgrfDLIVAADVLTYLGDLAAVFAGVARALKPG-GLFIFSVE------------------ 145
                         170       180
                  ....*....|....*....|....*....
gi 1864203801 265 TLQNAHNFYFSRKSLANVLTMSGFGIRRI 293
Cdd:COG4976   146 DADGSGRYAHSLDYVRDLLAAAGFEVPGL 174
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
139-246 2.89e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.54  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 139 RYLGDDVHWGPGTRILEVGTGAGGTLEYLCRD-GAIGLGLDLDASYLEYGRQRW------LNLRLETIDHLKLSFRP--D 209
Cdd:COG2230    41 DLILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAaeaglaDRVEVRLADYRDLPADGqfD 120
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1864203801 210 LVIYRHVLEHL--DNPIEELRKIAAICRRGtGMLYVEVP 246
Cdd:COG2230   121 AIVSIGMFEHVgpENYPAYFAKVARLLKPG-GRLLLHTP 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
152-245 4.03e-07

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: 47.81  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 152 RILEVGTGAGG-TLEYLCRDGAIGLGLDLDASYLEYGRQRWLNLRLETIDHLKLSF---------RPDLVIYRHVLEHL- 220
Cdd:cd02440     1 RVLDLGCGTGAlALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAeelppeadeSFDVIISDPPLHHLv 80
                          90       100
                  ....*....|....*....|....*
gi 1864203801 221 DNPIEELRKIAAICRRGtGMLYVEV 245
Cdd:cd02440    81 EDLARFLEEARRLLKPG-GVLVLTL 104
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
149-236 5.09e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 149 PGTRILEVGTGAGGTLEYLC-RDGAIGLGLDLDASYLEYGRQRWLNLRLETIDHLKLSF---------RPDLVIYRHVLE 218
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLaeldplpaeSFDLVVAFGVLH 105
                          90
                  ....*....|....*...
gi 1864203801 219 HLdnPIEELRKIAAICRR 236
Cdd:COG0500   106 HL--PPEEREALLRELAR 121
PRK08317 PRK08317
hypothetical protein; Provisional
131-237 9.67e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.31  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864203801 131 QRIGARIRRYLgddvHWGPGTRILEVGTGAGGTLEYLCRD-GAIG--LGLDLDASYLEYGRQRW----LNLRLETIDHLK 203
Cdd:PRK08317    5 RRYRARTFELL----AVQPGDRVLDVGCGPGNDARELARRvGPEGrvVGIDRSEAMLALAKERAaglgPNVEFVRGDADG 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1864203801 204 LSFRP---DLVIYRHVLEHLDNPIEELRKIAAICRRG 237
Cdd:PRK08317   81 LPFPDgsfDAVRSDRVLQHLEDPARALAEIARVLRPG 117
 
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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