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Conserved domains on  [gi|488421753|ref|WP_002491138|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Staphylococcus]

Protein Classification

class I SAM-dependent DNA methyltransferase( domain architecture ID 11471966)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047
PubMed:  23180741|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
4-136 1.97e-31

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


:

Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 113.94  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   4 YEDMSLVYDQ-LTQDQPYHSWFNIVQHFL----PSDSHDLLDIGCGTGNLTQLLTSLG-EVTGMDISVDMLSIASQKTNQ 77
Cdd:COG4976   11 FDQYADSYDAaLVEDLGYEAPALLAEELLarlpPGPFGRVLDLGCGTGLLGEALRPRGyRLTGVDLSEEMLAKAREKGVY 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  78 VKWIEGNMTHF-NLNKKFNMItIFCDSLNYLETLNDVkmtFERVYQHLNKNGVFIFDVHT 136
Cdd:COG4976   91 DRLLVADLADLaEPDGRFDLI-VAADVLTYLGDLAAV---FAGVARALKPGGLFIFSVED 146
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
4-136 1.97e-31

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 113.94  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   4 YEDMSLVYDQ-LTQDQPYHSWFNIVQHFL----PSDSHDLLDIGCGTGNLTQLLTSLG-EVTGMDISVDMLSIASQKTNQ 77
Cdd:COG4976   11 FDQYADSYDAaLVEDLGYEAPALLAEELLarlpPGPFGRVLDLGCGTGLLGEALRPRGyRLTGVDLSEEMLAKAREKGVY 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  78 VKWIEGNMTHF-NLNKKFNMItIFCDSLNYLETLNDVkmtFERVYQHLNKNGVFIFDVHT 136
Cdd:COG4976   91 DRLLVADLADLaEPDGRFDLI-VAADVLTYLGDLAAV---FAGVARALKPGGLFIFSVED 146
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-128 6.67e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 70.67  E-value: 6.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   39 LDIGCGTGNLTQLLTSLG--EVTGMDISVDMLSIASQKTNQ----VKWIEGNMTHFNL-NKKFNMITIFCdSLNYLeTLN 111
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGgaRVTGVDLSPEMLERARERAAEaglnVEFVQGDAEDLPFpDGSFDLVVSSG-VLHHL-PDP 79

                          90
                  ....*....|....*..
gi 488421753  112 DVKMTFERVYQHLNKNG 128
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 37-137 6.34e-11

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: 57.83  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  37 DLLDIGCGTGNLTQLLTSLG--EVTGMDISVDMLSIASQKT-----NQVKWIEGNMTHFNL--NKKFNMItIFCDSLNYL 107
Cdd:cd02440    1 RVLDLGCGTGALALALASGPgaRVTGVDISPVALELARKAAaallaDNVEVLKGDAEELPPeaDESFDVI-ISDPPLHHL 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 488421753 108 ETlnDVKMTFERVYQHLNKNGVFIFDVHTV 137
Cdd:cd02440   80 VE--DLARFLEEARRLLKPGGVLVLTLVLA 107
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 39-179 6.99e-11

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 60.38  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   39 LDIGCGTGNLTQLLTSLG---EVTGMDISVDMLSIASQKTN-QVKWIEGNMTHFNLNK-KFNMitIFCDSLnyLETLNDV 113
Cdd:TIGR02072  39 LDIGCGTGYLTRALLKRFpqaEFIALDISAGMLAQAKTKLSeNVQFICGDAEKLPLEDsSFDL--IVSNLA--LQWCDDL 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488421753  114 KMTFERVYQHLNKNGVFIFDV---HTVHKMKTLFNNKS--YLDESDnvfvgWDAICGEEPLSVYHEMTFFV 179
Cdd:TIGR02072 115 SQALSELARVLKPGGLLAFSTfgpGTLHELRQSFGQHGlrYLSLDE-----LKALLKNSFELLTLEEELIT 180
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 38-99 1.16e-09

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 56.70  E-value: 1.16e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488421753  38 LLDIGCGTGNLTQLLT----SLGEVTGMDISVDMLSIASQKT------NQVKWIEGNMTH--FNlNKKFNMITI 99
Cdd:PRK00216  55 VLDLACGTGDLAIALAkavgKTGEVVGLDFSEGMLAVGREKLrdlglsGNVEFVQGDAEAlpFP-DNSFDAVTI 127
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
4-136 1.97e-31

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 113.94  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   4 YEDMSLVYDQ-LTQDQPYHSWFNIVQHFL----PSDSHDLLDIGCGTGNLTQLLTSLG-EVTGMDISVDMLSIASQKTNQ 77
Cdd:COG4976   11 FDQYADSYDAaLVEDLGYEAPALLAEELLarlpPGPFGRVLDLGCGTGLLGEALRPRGyRLTGVDLSEEMLAKAREKGVY 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  78 VKWIEGNMTHF-NLNKKFNMItIFCDSLNYLETLNDVkmtFERVYQHLNKNGVFIFDVHT 136
Cdd:COG4976   91 DRLLVADLADLaEPDGRFDLI-VAADVLTYLGDLAAV---FAGVARALKPGGLFIFSVED 146
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
39-134 1.20e-21

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 85.65  E-value: 1.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  39 LDIGCGTGNLTQLLTSL---GEVTGMDISVDMLSIASQKTNQVKWIEGNMTHFNLNKKFNMItIFCDSLNYLETLNDVkm 115
Cdd:COG4106    6 LDLGCGTGRLTALLAERfpgARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEPFDLV-VSNAALHWLPDHAAL-- 82

                         90
                 ....*....|....*....
gi 488421753 116 tFERVYQHLNKNGVFIFDV 134
Cdd:COG4106   83 -LARLAAALAPGGVLAVQV 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 15-134 6.11e-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: 74.28  E-value: 6.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  15 TQDQPYHSW----FNIVQHFLPSDSHdLLDIGCGTGNLTQLLTSLG-EVTGMDISVDMLSIASQKTNQ--VKWIEGNMTH 87
Cdd:COG2227    2 SDPDARDFWdrrlAALLARLLPAGGR-VLDVGCGTGRLALALARRGaDVTGVDISPEALEIARERAAElnVDFVQGDLED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488421753  88 FNL-NKKFNMITifcdSLNYLETLNDVKMTFERVYQHLNKNGVFIFDV 134
Cdd:COG2227   81 LPLeDGSFDLVI----CSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 20-143 2.37e-16

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: 73.10  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  20 YHSWFNIVQHFLPSDSHDLLDIGCGTGNLTQLLTSLG-EVTGMDISVDMLSIASQKTN----QVKWIEGNMTHFNL-NKK 93
Cdd:COG2226    8 YDGREALLAALGLRPGARVLDLGCGTGRLALALAERGaRVTGVDISPEMLELARERAAeaglNVEFVVGDAEDLPFpDGS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488421753  94 FNMITIFCdSLNYLEtlnDVKMTFERVYQHLNKNGVFIFDVHTVHKMKTL 143
Cdd:COG2226   88 FDLVISSF-VLHHLP---DPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-128 6.67e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 70.67  E-value: 6.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   39 LDIGCGTGNLTQLLTSLG--EVTGMDISVDMLSIASQKTNQ----VKWIEGNMTHFNL-NKKFNMITIFCdSLNYLeTLN 111
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGgaRVTGVDLSPEMLERARERAAEaglnVEFVQGDAEDLPFpDGSFDLVVSSG-VLHHL-PDP 79

                          90
                  ....*....|....*..
gi 488421753  112 DVKMTFERVYQHLNKNG 128
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 39-132 1.33e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.61  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   39 LDIGCGTGNLTQLLTSLG-EVTGMDISVDMLSIASQKT--NQVKWIEGNMTHFNL-NKKFNMITifcdSLNYLETLNDVK 114
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGaRVTGVDISPEMLELAREKAprEGLTFVVGDAEDLPFpDNSFDLVL----SSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 488421753  115 MTFERVYQHLNKNGVFIF 132
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 39-130 8.29e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 59.69  E-value: 8.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   39 LDIGCGTGNLTQLL---TSLGEVTGMDISVDMLSIASQKTN--------QVKWIEGNMtHFNLNKKFNMITIFcdslNYL 107
Cdd:pfam08242   1 LEIGCGTGTLLRALleaLPGLEYTGLDISPAALEAARERLAalgllnavRVELFQLDL-GELDPGSFDVVVAS----NVL 75

                          90       100
                  ....*....|....*....|...
gi 488421753  108 ETLNDVKMTFERVYQHLNKNGVF 130
Cdd:pfam08242  76 HHLADPRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 18-135 3.11e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 60.70  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  18 QPYHSWFNIVQHFLPSDSHdLLDIGCGTGNLTQLLTSL--GEVTGMDISVDMLSIA-----SQKTNQVKWIEGNMTHFN- 89
Cdd:COG0500   11 LPGLAALLALLERLPKGGR-VLDLGCGTGRNLLALAARfgGRVIGIDLSPEAIALAraraaKAGLGNVEFLVADLAELDp 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488421753  90 -LNKKFNMItIFCDSLNYLETLNDVKmTFERVYQHLNKNGVFIFDVH 135
Cdd:COG0500   90 lPAESFDLV-VAFGVLHHLPPEEREA-LLRELARALKPGGVLLLSAS 134
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 37-137 6.34e-11

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: 57.83  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  37 DLLDIGCGTGNLTQLLTSLG--EVTGMDISVDMLSIASQKT-----NQVKWIEGNMTHFNL--NKKFNMItIFCDSLNYL 107
Cdd:cd02440    1 RVLDLGCGTGALALALASGPgaRVTGVDISPVALELARKAAaallaDNVEVLKGDAEELPPeaDESFDVI-ISDPPLHHL 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 488421753 108 ETlnDVKMTFERVYQHLNKNGVFIFDVHTV 137
Cdd:cd02440   80 VE--DLARFLEEARRLLKPGGVLVLTLVLA 107
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 39-179 6.99e-11

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 60.38  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   39 LDIGCGTGNLTQLLTSLG---EVTGMDISVDMLSIASQKTN-QVKWIEGNMTHFNLNK-KFNMitIFCDSLnyLETLNDV 113
Cdd:TIGR02072  39 LDIGCGTGYLTRALLKRFpqaEFIALDISAGMLAQAKTKLSeNVQFICGDAEKLPLEDsSFDL--IVSNLA--LQWCDDL 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488421753  114 KMTFERVYQHLNKNGVFIFDV---HTVHKMKTLFNNKS--YLDESDnvfvgWDAICGEEPLSVYHEMTFFV 179
Cdd:TIGR02072 115 SQALSELARVLKPGGLLAFSTfgpGTLHELRQSFGQHGlrYLSLDE-----LKALLKNSFELLTLEEELIT 180
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-152 2.34e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 57.44  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   37 DLLDIGCGTGNLTQLLTSLG-EVTGMDISVDMLSIAsqKTNQVKWIEGNMTHFNLNKKFNMITifcdSLNYLETLNDVKM 115
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRAQGfSVTGVDPSPIAIERA--LLNVRFDQFDEQEAAVPAGKFDVIV----AREVLEHVPDPPA 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488421753  116 TFERVYQHLNKNGVFIFDVHTV-HKMKTLFNNKSYLDE 152
Cdd:pfam13489  99 LLRQIAALLKPGGLLLLSTPLAsDEADRLLLEWPYLRP 136
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 38-99 1.16e-09

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 56.70  E-value: 1.16e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488421753  38 LLDIGCGTGNLTQLLT----SLGEVTGMDISVDMLSIASQKT------NQVKWIEGNMTH--FNlNKKFNMITI 99
Cdd:PRK00216  55 VLDLACGTGDLAIALAkavgKTGEVVGLDFSEGMLAVGREKLrdlglsGNVEFVQGDAEAlpFP-DNSFDAVTI 127
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 38-131 3.61e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 53.96  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   38 LLDIGCGTGNLTQLLTSL----GEVTGMDISVDMLSIASQKTNQ-----VKWIEGNMTHFNLN---KKFNMITIFCdSLN 105
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEElgpnAEVVGIDISEEAIEKARENAQKlgfdnVEFEQGDIEELPELledDKFDVVISNC-VLN 85

                          90       100
                  ....*....|....*....|....*.
gi 488421753  106 YLETLNDVKMTFERVyqhLNKNGVFI 131
Cdd:pfam13847  86 HIPDPDKVLQEILRV---LKPGGRLI 108
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 26-132 1.51e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.24  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753  26 IVQHFLPSDSHDLLDIGCGTGNLTQLLTSLG--EVTGMDISVDMLSIASQK------TNQVKWIEGNMTHFNLNKKFNMI 97
Cdd:COG2230   43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRYgvRVTGVTLSPEQLEYARERaaeaglADRVEVRLADYRDLPADGQFDAI 122

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488421753  98 TifcdSLNYLETLND--VKMTFERVYQHLNKNGVFIF 132
Cdd:COG2230  123 V----SIGMFEHVGPenYPAYFAKVARLLKPGGRLLL 155
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 40-88 5.68e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 49.17  E-value: 5.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488421753  40 DIGCGTGNLTQLLTS---LGEVTGMDISVDMLSIASQKTNQVKWIEGNMTHF 88
Cdd:PRK01683  37 DLGCGPGNSTELLVErwpAARITGIDSSPAMLAEARSRLPDCQFVEADIASW 88
PRK08317 PRK08317
hypothetical protein; Provisional
 39-75 1.22e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.85  E-value: 1.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 488421753  39 LDIGCGTGNLTQLL----TSLGEVTGMDISVDMLSIASQKT 75
Cdd:PRK08317  24 LDVGCGPGNDARELarrvGPEGRVVGIDRSEAMLALAKERA 64
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 37-99 1.80e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 41.80  E-value: 1.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488421753  37 DLLDIGCGTGNLTQLLT----SLGEVTGMDISVDMLSIASQKTNQ--------VKWIEGNMTHFNLNK-KFNMITI 99
Cdd:PLN02233  76 RVLDLCCGSGDLAFLLSekvgSDGKVMGLDFSSEQLAVAASRQELkakscyknIEWIEGDATDLPFDDcYFDAITM 151
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 39-134 2.87e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 40.26  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488421753   39 LDIGCGTGNLTQLLTSLGE--VTGMDIsVDMLSIASQKTNQVKWIEGNMTHFN--------LNKKFNMIT----IFCDSL 104
Cdd:pfam01728  26 LDLGAAPGGWSQVALQRGAgkVVGVDL-GPMQLWKPRNDPGVTFIQGDIRDPEtldlleelLGRKVDLVLsdgsPFISGN 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 488421753  105 NYLETLND---VKMTFERVYQHLNKNGVFIFDV 134
Cdd:pfam01728 105 KVLDHLRSldlVKAALEVALELLRKGGNFVCKV 137
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
39-84 4.74e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 40.12  E-value: 4.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488421753   39 LDIGCGTGNLTQLLTSL----GEVTGMDISVDMLSIASQKTN-----QVKWIEGN 84
Cdd:pfam01209  47 LDVAGGTGDWTFGLSDSagssGKVVGLDINENMLKEGEKKAKeegkyNIEFLQGN 101
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 25-64 7.90e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 39.89  E-value: 7.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488421753  25 NIVQHFLPSDSHDLLDIGCGTGNLT-QLLTSLGEVT-----GMDIS 64
Cdd:PRK11088  76 NLLAERLDEKATALLDIGCGEGYYThALADALPEITtmqlfGLDIS 121
 
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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