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Conserved domains on  [gi|1986748763|gb|QRQ79622|]
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class I SAM-dependent methyltransferase [Glutamicibacter protophormiae]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 26-168 5.47e-23

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: 91.21  E-value: 5.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  26 FQSGADSYDKIRpsyppQALDFALQARPRTAVDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLAERLP----QVARTC 101
Cdd:COG2226     1 FDRVAARYDGRE-----ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAeaglNVEFVV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1986748763 102 AAGEDTGLPENAFDLVSYAQAWHWV-DHAKASAEAARLLRNDGWLTLlwnqLNVTIPWVHRLARIMHA 168
Cdd:COG2226    76 GDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVV----VDFSPPDLAELEELLAE 139
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 26-168 5.47e-23

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: 91.21  E-value: 5.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  26 FQSGADSYDKIRpsyppQALDFALQARPRTAVDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLAERLP----QVARTC 101
Cdd:COG2226     1 FDRVAARYDGRE-----ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAeaglNVEFVV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1986748763 102 AAGEDTGLPENAFDLVSYAQAWHWV-DHAKASAEAARLLRNDGWLTLlwnqLNVTIPWVHRLARIMHA 168
Cdd:COG2226    76 GDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVV----VDFSPPDLAELEELLAE 139
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-145 1.55e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 85.79  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  57 VDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLAERLPQVART--CAAGEDTGLPENAFDLVSYAQAWHWV-DHAKASA 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTfvVGDAEDLPFPDNSFDLVLSSEVLHHVeDPERALR 80

                          90
                  ....*....|..
gi 1986748763 134 EAARLLRNDGWL 145
Cdd:pfam08241  81 EIARVLKPGGIL 92
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 53-145 6.29e-10

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: 57.68  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  53 PRTAVDIGCGSGIFTEQLASRGLEVS--AVDPSADMLRVLAERLP-QVARTCAAGEDTGLPENAFDLVSYAQAWHWVDHA 129
Cdd:TIGR02072  35 PASVLDIGCGTGYLTRALLKRFPQAEfiALDISAGMLAQAKTKLSeNVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDL 114

                          90
                  ....*....|....*..
gi 1986748763 130 KAS-AEAARLLRNDGWL 145
Cdd:TIGR02072 115 SQAlSELARVLKPGGLL 131
PRK08317 PRK08317
hypothetical protein; Provisional
 48-168 3.33e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 55.71  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  48 ALQARP-RTAVDIGCGSGIFTEQLASR---GLEVSAVDPSADMLRVLAER----LPQVARTCAAGEDTGLPENAFDLVSY 119
Cdd:PRK08317   14 LLAVQPgDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERaaglGPNVEFVRGDADGLPFPDGSFDAVRS 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1986748763 120 AQAW-HWVDHAKASAEAARLLRNDGWLTLL---WNQLNVTIPWVHRLARIMHA 168
Cdd:PRK08317   94 DRVLqHLEDPARALAEIARVLRPGGRVVVLdtdWDTLVWHSGDRALMRKILNF 146
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 55-145 3.86e-09

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: 53.20  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  55 TAVDIGCGSGIFTEQLASR-GLEVSAVDPSADMLRVL----AERLPQVAR--TCAAGEDTGLPENAFDLVSYAQAWHWVD 127
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELArkaaAALLADNVEvlKGDAEELPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|
gi 1986748763 128 HAKASA--EAARLLRNDGWL 145
Cdd:cd02440    81 EDLARFleEARRLLKPGGVL 100
rADc smart00650
Ribosomal RNA adenine dimethylases;
55-99 2.47e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.88  E-value: 2.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1986748763   55 TAVDIGCGSGIFTEQLASRGLEVSAV--DPsaDMLRVLAERLPQVAR 99
Cdd:smart00650  16 TVLEIGPGKGALTEELLERAKRVTAIeiDP--RLAPRLREKFAAADN 60
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 26-168 5.47e-23

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: 91.21  E-value: 5.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  26 FQSGADSYDKIRpsyppQALDFALQARPRTAVDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLAERLP----QVARTC 101
Cdd:COG2226     1 FDRVAARYDGRE-----ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAeaglNVEFVV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1986748763 102 AAGEDTGLPENAFDLVSYAQAWHWV-DHAKASAEAARLLRNDGWLTLlwnqLNVTIPWVHRLARIMHA 168
Cdd:COG2226    76 GDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVV----VDFSPPDLAELEELLAE 139
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-145 1.55e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 85.79  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  57 VDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLAERLPQVART--CAAGEDTGLPENAFDLVSYAQAWHWV-DHAKASA 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTfvVGDAEDLPFPDNSFDLVLSSEVLHHVeDPERALR 80

                          90
                  ....*....|..
gi 1986748763 134 EAARLLRNDGWL 145
Cdd:pfam08241  81 EIARVLKPGGIL 92
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
52-145 3.66e-19

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 79.87  E-value: 3.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  52 RPRTAVDIGCGSGIFTEQLASR--GLEVSAVDPSADMLRVLAERLPQVARTCAAGEDTGLPENaFDLVSYAQAWHWV-DH 128
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEP-FDLVVSNAALHWLpDH 79

                          90
                  ....*....|....*..
gi 1986748763 129 AKASAEAARLLRNDGWL 145
Cdd:COG4106    80 AALLARLAAALAPGGVL 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 51-145 1.03e-18

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: 79.29  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  51 ARPRTAVDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLAERLPQVART--CAAGEDTGLPENAFDLVSYAQAWHWV-D 127
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDfvQGDLEDLPLEDGSFDLVICSEVLEHLpD 102

                          90
                  ....*....|....*...
gi 1986748763 128 HAKASAEAARLLRNDGWL 145
Cdd:COG2227   103 PAALLRELARLLKPGGLL 120
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 58-143 1.42e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 75.68  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  58 DIGCGSGIFTEQLASR-GLEVSAVDPSADMLRVLAERL----PQVARTCAAGEDTGLPENAFDLVSYAQAWHWV---DHA 129
Cdd:pfam13649   3 DLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdpDLE 82

                          90
                  ....*....|....
gi 1986748763 130 KASAEAARLLRNDG 143
Cdd:pfam13649  83 AALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
21-145 1.50e-14

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 69.64  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  21 ELASAFQSGADSYDKI---RPSY--PPQALDFALQA----RPRTAVDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLA 91
Cdd:COG4976     6 YVEALFDQYADSYDAAlveDLGYeaPALLAEELLARlppgPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1986748763  92 ERLPQVARTCAAGEDTGLPENAFDLVSyaqAW----HWVDHAKASAEAARLLRNDGWL 145
Cdd:COG4976    86 EKGVYDRLLVADLADLAEPDGRFDLIV---AAdvltYLGDLAAVFAGVARALKPGGLF 140
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 33-145 3.46e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 66.48  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  33 YDKIRPSYPPQALDFALQARPRTAVDIGCGSGIFTEQLASR-GLEVSAVDPSADMLRVLAERLPQVA------RTCAAGE 105
Cdd:COG0500     7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGlgnvefLVADLAE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1986748763 106 DTGLPENAFDLVSYAQAWHWVDHAKAS---AEAARLLRNDGWL 145
Cdd:COG0500    87 LDPLPAESFDLVVAFGVLHHLPPEEREallRELARALKPGGVL 129
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 57-145 3.28e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 58.53  E-value: 3.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  57 VDIGCGSGIFTEQLA--SRGLEVSAVDPSADMLRVLAERLPQVARTCAA------GEDTGLPENAFDLVSYAQAWHWVDH 128
Cdd:pfam08242   1 LEIGCGTGTLLRALLeaLPGLEYTGLDISPAALEAARERLAALGLLNAVrvelfqLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1986748763 129 AKASAE-AARLLRNDGWL 145
Cdd:pfam08242  81 PRAVLRnIRRLLKPGGVL 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 53-145 6.29e-10

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: 57.68  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  53 PRTAVDIGCGSGIFTEQLASRGLEVS--AVDPSADMLRVLAERLP-QVARTCAAGEDTGLPENAFDLVSYAQAWHWVDHA 129
Cdd:TIGR02072  35 PASVLDIGCGTGYLTRALLKRFPQAEfiALDISAGMLAQAKTKLSeNVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDL 114

                          90
                  ....*....|....*..
gi 1986748763 130 KAS-AEAARLLRNDGWL 145
Cdd:TIGR02072 115 SQAlSELARVLKPGGLL 131
PRK08317 PRK08317
hypothetical protein; Provisional
 48-168 3.33e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 55.71  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  48 ALQARP-RTAVDIGCGSGIFTEQLASR---GLEVSAVDPSADMLRVLAER----LPQVARTCAAGEDTGLPENAFDLVSY 119
Cdd:PRK08317   14 LLAVQPgDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERaaglGPNVEFVRGDADGLPFPDGSFDAVRS 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1986748763 120 AQAW-HWVDHAKASAEAARLLRNDGWLTLL---WNQLNVTIPWVHRLARIMHA 168
Cdd:PRK08317   94 DRVLqHLEDPARALAEIARVLRPGGRVVVLdtdWDTLVWHSGDRALMRKILNF 146
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 55-145 3.86e-09

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: 53.20  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  55 TAVDIGCGSGIFTEQLASR-GLEVSAVDPSADMLRVL----AERLPQVAR--TCAAGEDTGLPENAFDLVSYAQAWHWVD 127
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELArkaaAALLADNVEvlKGDAEELPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|
gi 1986748763 128 HAKASA--EAARLLRNDGWL 145
Cdd:cd02440    81 EDLARFleEARRLLKPGGVL 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 33-165 6.28e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 53.59  E-value: 6.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  33 YDKIRPSYPPQALDFALQARPRTA--VDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLaerLPQVARTCAAGEDTGLP 110
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGrvLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERA---LLNVRFDQFDEQEAAVP 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1986748763 111 ENAFDLVSYAQAWHWV-DHAKASAEAARLLRNDGWLTLLwnQLNVTIPWVHRLARI 165
Cdd:pfam13489  78 AGKFDVIVAREVLEHVpDPPALLRQIAALLKPGGLLLLS--TPLASDEADRLLLEW 131
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 48-148 5.84e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 49.00  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  48 ALQARPR-TAVDIGCGSGIFTEQLASRGL---EVSAVDPSADMLRVLAERL------PQVARTCAAGEDTGLPENAFDLV 117
Cdd:PRK00216   46 WLGVRPGdKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGMLAVGREKLrdlglsGNVEFVQGDAEALPFPDNSFDAV 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1986748763 118 SYAqaw-hwVDHAKASAEAARLLRNDGWLTLL 148
Cdd:PRK00216  126 TIAfglrnvPDIDKALREMYRVLKPGGRLVIL 157
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 52-130 6.58e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 49.17  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  52 RPRTAVDIGCGSGIFTEQLASR--GLEVSAVDPSADMLRVLAERLPQVARTCAageDTG--LPENAFDLVsYAQA-WHWV 126
Cdd:PRK01683   31 NPRYVVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLPDCQFVEA---DIAswQPPQALDLI-FANAsLQWL 106


                  ....*
gi 1986748763 127 -DHAK 130
Cdd:PRK01683  107 pDHLE 111
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 46-178 1.12e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 45.14  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  46 DFALQARPRTAVDIGCGSGIFTEQLASR--GLEVSAVD---PSADMLRV------LAER-------LPQVARTcaagedt 107
Cdd:COG4123    31 AFAPVKKGGRVLDLGTGTGVIALMLAQRspGARITGVEiqpEAAELARRnvalngLEDRitvihgdLKEFAAE------- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763 108 gLPENAFDLV------------------SYAQAWH--------WVDHakasaeAARLLRNDGWLTLLWnqlnvtipWVHR 161
Cdd:COG4123   104 -LPPGSFDLVvsnppyfkagsgrkspdeARAIARHedaltledLIRA------AARLLKPGGRFALIH--------PAER 168

                         170
                  ....*....|....*..
gi 1986748763 162 LARIMHAGDVHRpeLEP 178
Cdd:COG4123   169 LAEILAALRKYG--LGP 183
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 48-147 2.23e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 43.38  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  48 ALQARP-RTAVDIGCGSGIFTEQLASR-GLEVSAVDPSADML-----RVLAERLPQVARTCAAG-EDTGlPENAFDLVSY 119
Cdd:COG2230    46 KLGLKPgMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLeyareRAAEAGLADRVEVRLADyRDLP-ADGQFDAIVS 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1986748763 120 AQAWHWVDHAKAS---AEAARLLRNDGWLTL 147
Cdd:COG2230   125 IGMFEHVGPENYPayfAKVARLLKPGGRLLL 155
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 54-96 5.03e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 43.29  E-value: 5.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1986748763  54 RTAVDIGCGSGIFTEQLASRGLEVSAVDPSADMLRVLAERLPQ 96
Cdd:PRK07580   65 LRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPE 107
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 43-145 1.68e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 41.82  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  43 QALDFALQARPRTAVDIGCGSGIFTEQLA-----SRGLEVSAVDPSADMLRVLAERLPQVARTCAAGEDTGLPENAFDLV 117
Cdd:PRK11088   76 NLLAERLDEKATALLDIGCGEGYYTHALAdalpeITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAI 155

                          90       100       110
                  ....*....|....*....|....*....|
gi 1986748763 118 S--YAQawhwvdhAKAsAEAARLLRNDGWL 145
Cdd:PRK11088  156 IriYAP-------CKA-EELARVVKPGGIV 177
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 57-139 1.52e-03

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 39.33  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  57 VDIGCGSGIFTEQLASRGLEVS---AVDPSADMLRVLAERLPQVART---CAAGEDTGLPENAFDLVSyaqAWHWVDHAK 130
Cdd:PLN02396  136 IDIGCGGGLLSEPLARMGATVTgvdAVDKNVKIARLHADMDPVTSTIeylCTTAEKLADEGRKFDAVL---SLEVIEHVA 212


                  ....*....
gi 1986748763 131 ASAEAARLL 139
Cdd:PLN02396  213 NPAEFCKSL 221
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 52-126 1.64e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 38.90  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  52 RPRTAVDIGCGSGIFTEQLASR--GLEVSAVDPSADMLRVLAERL----PQVARTCAAGEDTGLpenafdLVSYAqAWHW 125
Cdd:PRK14103   29 RARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAARERGvdarTGDVRDWKPKPDTDV------VVSNA-ALQW 101


                  .
gi 1986748763 126 V 126
Cdd:PRK14103  102 V 102
rADc smart00650
Ribosomal RNA adenine dimethylases;
55-99 2.47e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.88  E-value: 2.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1986748763   55 TAVDIGCGSGIFTEQLASRGLEVSAV--DPsaDMLRVLAERLPQVAR 99
Cdd:smart00650  16 TVLEIGPGKGALTEELLERAKRVTAIeiDP--RLAPRLREKFAAADN 60
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 45-150 3.34e-03

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 37.48  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  45 LDFALQARPRTAVDIGCGSGIFTEQLASR--GLEVSAVDPSADMLRvLAER-----LPQVARTCAAGEDTGLPENAFDLV 117
Cdd:COG2813    42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVE-LARAnaaanGLENVEVLWSDGLSGVPDGSFDLI 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1986748763 118 ------------SYAQAWHWVdhakasAEAARLLRNDGWLTLLWN 150
Cdd:COG2813   121 lsnppfhagravDKEVAHALI------ADAARHLRPGGELWLVAN 159
PLN02244 PLN02244
tocopherol O-methyltransferase
 44-161 6.93e-03

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 37.42  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1986748763  44 ALDFALQARPRTAVDIGCGSGIFTEQLASR-GLEVSAVDPSAdmlrVLAERLPQVARTCAAGE----------DTGLPEN 112
Cdd:PLN02244  110 GVPDDDEKRPKRIVDVGCGIGGSSRYLARKyGANVKGITLSP----VQAARANALAAAQGLSDkvsfqvadalNQPFEDG 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1986748763 113 AFDLV-SYAQAWHWVDHAKASAEAARLLRNDGWLTLlwnqlnVTipWVHR 161
Cdd:PLN02244  186 QFDLVwSMESGEHMPDKRKFVQELARVAAPGGRIII------VT--WCHR 227
 
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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