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Conserved domains on  [gi|489502777|ref|WP_003407670|]
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MULTISPECIES: phthiotriol/phenolphthiotriol dimycocerosates methyltransferase [Mycobacterium]

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

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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]; ...
 161-279 3.05e-31

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: 115.09  E-value: 3.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNlgPASYTGLDLNPASIDLCRAKHRLPGL--QFVQGDAQNLPFPDESFDAVVNVEASHQY 238
Cdd:COG2226   23 GARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLnvEFVVGDAEDLPFPDGSFDLVISSFVLHHL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489502777 239 PDFRGFLAEVARVLRPGGHFLYTDSRRnPVVAEWEAALADA 279
Cdd:COG2226  101 PDPERALAEIARVLKPGGRLVVVDFSP-PDLAELEELLAEA 140
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 161-279 3.05e-31

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: 115.09  E-value: 3.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNlgPASYTGLDLNPASIDLCRAKHRLPGL--QFVQGDAQNLPFPDESFDAVVNVEASHQY 238
Cdd:COG2226   23 GARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLnvEFVVGDAEDLPFPDGSFDLVISSFVLHHL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489502777 239 PDFRGFLAEVARVLRPGGHFLYTDSRRnPVVAEWEAALADA 279
Cdd:COG2226  101 PDPERALAEIARVLKPGGRLVVVDFSP-PDLAELEELLAEA 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 165-259 1.25e-29

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 108.91  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  165 LEVSCGAGGGASYIARNLgpASYTGLDLNPASIDLCRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQYPDFRGF 244
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*
gi 489502777  245 LAEVARVLRPGGHFL 259
Cdd:pfam08241  79 LREIARVLKPGGILI 93
PRK08317 PRK08317
hypothetical protein; Provisional
 161-321 3.37e-22

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 93.46  E-value: 3.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGPAS-YTGLDLNPASIDLC--RAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQ 237
Cdd:PRK08317  20 GDRVLDVGCGPGNDARELARRVGPEGrVVGIDRSEAMLALAkeRAAGLGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQH 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 238 YPDFRGFLAEVARVLRPGGHFLYTDSrrnpvvaEWEAALADAPLRTISQRDIgaqakRGLDANTARSQeaIGRRAPVLL- 316
Cdd:PRK08317 100 LEDPARALAEIARVLRPGGRVVVLDT-------DWDTLVWHSGDRALMRKIL-----NFWSDHFADPW--LGRRLPGLFr 165


                 ....*.
gi 489502777 317 -AGLTR 321
Cdd:PRK08317 166 eAGLTD 171
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 161-259 1.49e-17

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 80.38  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  161 GKEVLEVSCGAGGGASYIARNLGP-ASYTGLDLNPASIDLCRAKHRLPG-LQFVQGDAQNLPFPDESFDAVV------NV 232
Cdd:TIGR01934  40 GQKVLDVACGTGDLAIELAKSAPDrGKVTGVDFSSEMLEVAKKKSELPLnIEFIQADAEALPFEDNSFDAVTiafglrNV 119

                          90       100
                  ....*....|....*....|....*..
gi 489502777  233 eashqyPDFRGFLAEVARVLRPGGHFL 259
Cdd:TIGR01934 120 ------TDIQKALREMYRVLKPGGRLV 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 164-261 3.43e-16

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: 73.23  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 164 VLEVSCGAGGGASYIARnLGPASYTGLDLNPASIDLCRAKHRL---PGLQFVQGDA-QNLPFPDESFDAVV-NVEASHQY 238
Cdd:cd02440    2 VLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAAllaDNVEVLKGDAeELPPEADESFDVIIsDPPLHHLV 80

                         90       100
                 ....*....|....*....|...
gi 489502777 239 PDFRGFLAEVARVLRPGGHFLYT 261
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
162-311 5.38e-10

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 58.58  E-value: 5.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777   162 KEVLEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCRAKHRLPGLQ----FVQGDAQNLPFPDEsFDAVVNVEASHQ 237
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQgrirIFYRDSAKDPFPDT-YDLVFGFEVIHH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777   238 YPDFRGFLAEVARVLRPGGHFLYTD--------------SRRNPVVAEWEAALADAPLRTISQRDIGAQAKRGL-DANTA 302
Cdd:smart00828  80 IKDKMDLFSNISRHLKDGGHLVLADfianllsaieheetTSYLVTREEWAELLARNNLRVVEGVDASLEIANFLyDPGFE 159


                   ....*....
gi 489502777   303 RSQEAIGRR 311
Cdd:smart00828 160 DNLERLYQD 168
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 161-279 3.05e-31

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: 115.09  E-value: 3.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNlgPASYTGLDLNPASIDLCRAKHRLPGL--QFVQGDAQNLPFPDESFDAVVNVEASHQY 238
Cdd:COG2226   23 GARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGLnvEFVVGDAEDLPFPDGSFDLVISSFVLHHL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489502777 239 PDFRGFLAEVARVLRPGGHFLYTDSRRnPVVAEWEAALADA 279
Cdd:COG2226  101 PDPERALAEIARVLKPGGRLVVVDFSP-PDLAELEELLAEA 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 165-259 1.25e-29

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 108.91  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  165 LEVSCGAGGGASYIARNLgpASYTGLDLNPASIDLCRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQYPDFRGF 244
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*
gi 489502777  245 LAEVARVLRPGGHFL 259
Cdd:pfam08241  79 LREIARVLKPGGILI 93
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 164-256 7.09e-28

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 104.57  E-value: 7.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  164 VLEVSCGAGGGASYIARNLGpASYTGLDLNPASIDLCRAKHRLPGL--QFVQGDAQNLPFPDESFDAVVNVEASH--QYP 239
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGLnvEFVQGDAEDLPFPDGSFDLVVSSGVLHhlPDP 79

                          90
                  ....*....|....*..
gi 489502777  240 DFRGFLAEVARVLRPGG 256
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 159-262 7.18e-26

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: 100.09  E-value: 7.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 159 LTGKEVLEVSCGAGGGASYIARnLGpASYTGLDLNPASIDLCRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQY 238
Cdd:COG2227   23 PAGGRVLDVGCGTGRLALALAR-RG-ADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHL 100

                         90       100
                 ....*....|....*....|....
gi 489502777 239 PDFRGFLAEVARVLRPGGHFLYTD 262
Cdd:COG2227  101 PDPAALLRELARLLKPGGLLLLST 124
PRK08317 PRK08317
hypothetical protein; Provisional
 161-321 3.37e-22

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 93.46  E-value: 3.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGPAS-YTGLDLNPASIDLC--RAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQ 237
Cdd:PRK08317  20 GDRVLDVGCGPGNDARELARRVGPEGrVVGIDRSEAMLALAkeRAAGLGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQH 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 238 YPDFRGFLAEVARVLRPGGHFLYTDSrrnpvvaEWEAALADAPLRTISQRDIgaqakRGLDANTARSQeaIGRRAPVLL- 316
Cdd:PRK08317 100 LEDPARALAEIARVLRPGGRVVVLDT-------DWDTLVWHSGDRALMRKIL-----NFWSDHFADPW--LGRRLPGLFr 165


                 ....*.
gi 489502777 317 -AGLTR 321
Cdd:PRK08317 166 eAGLTD 171
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
164-259 1.94e-19

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 82.18  E-value: 1.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 164 VLEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCRAkhRLPGLQFVQGDAQNLPfPDESFDAVVNVEASHQYPDFRG 243
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARA--RLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLPDHAA 81

                         90
                 ....*....|....*.
gi 489502777 244 FLAEVARVLRPGGHFL 259
Cdd:COG4106   82 LLARLAAALAPGGVLA 97
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 161-262 4.30e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 83.06  E-value: 4.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGpASYTGLDLNPASIDLCRAKHRLPGL----QFVQGDAQNLPfPDESFDAVVNVEASH 236
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEAGLadrvEVRLADYRDLP-ADGQFDAIVSIGMFE 129

                         90       100
                 ....*....|....*....|....*...
gi 489502777 237 QYPD--FRGFLAEVARVLRPGGHFLYTD 262
Cdd:COG2230  130 HVGPenYPAYFAKVARLLKPGGRLLLHT 157
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 161-259 1.49e-17

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 80.38  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  161 GKEVLEVSCGAGGGASYIARNLGP-ASYTGLDLNPASIDLCRAKHRLPG-LQFVQGDAQNLPFPDESFDAVV------NV 232
Cdd:TIGR01934  40 GQKVLDVACGTGDLAIELAKSAPDrGKVTGVDFSSEMLEVAKKKSELPLnIEFIQADAEALPFEDNSFDAVTiafglrNV 119

                          90       100
                  ....*....|....*....|....*..
gi 489502777  233 eashqyPDFRGFLAEVARVLRPGGHFL 259
Cdd:TIGR01934 120 ------TDIQKALREMYRVLKPGGRLV 140
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 161-259 3.74e-17

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 79.43  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGP-ASYTGLDLNPASIDLCRAKHR----LPGLQFVQGDAQNLPFPDESFDAVV----- 230
Cdd:PRK00216  52 GDKVLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAVGREKLRdlglSGNVEFVQGDAEALPFPDNSFDAVTiafgl 131

                         90       100       110
                 ....*....|....*....|....*....|
gi 489502777 231 -NVeashqyPDFRGFLAEVARVLRPGGHFL 259
Cdd:PRK00216 132 rNV------PDIDKALREMYRVLKPGGRLV 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 161-317 6.89e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 78.03  E-value: 6.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGpASYTGLDLNPASIDLCRAKHR---LPGLQFVQGD-AQNLPFPDESFDAVVNVEASH 236
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARAAkagLGNVEFLVADlAELDPLPAESFDLVVAFGVLH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 237 QYP--DFRGFLAEVARVLRPGGHFLYTDSRRNPVVAEWEAALADAPLRTISQRDIGAQAKRGLDANTARSQEAIGRRAPV 314
Cdd:COG0500  106 HLPpeEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLRLLALELYLRALLAAAATEDLRSDA 185


                 ...
gi 489502777 315 LLA 317
Cdd:COG0500  186 LLE 188
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 164-261 3.43e-16

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: 73.23  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 164 VLEVSCGAGGGASYIARnLGPASYTGLDLNPASIDLCRAKHRL---PGLQFVQGDA-QNLPFPDESFDAVV-NVEASHQY 238
Cdd:cd02440    2 VLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAAllaDNVEVLKGDAeELPPEADESFDVIIsDPPLHHLV 80

                         90       100
                 ....*....|....*....|...
gi 489502777 239 PDFRGFLAEVARVLRPGGHFLYT 261
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 161-264 2.00e-15

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 72.45  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  161 GKEVLEVSCGAGGGASYIARNLGP-ASYTGLDLNPASIDLCR---AKHRLPGLQFVQGDAQNLP--FPDESFDAVVNVEA 234
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEELGPnAEVVGIDISEEAIEKARenaQKLGFDNVEFEQGDIEELPelLEDDKFDVVISNCV 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 489502777  235 SHQYPDFRGFLAEVARVLRPGGHFLYTDSR 264
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
PLN02244 PLN02244
tocopherol O-methyltransferase
 162-256 9.22e-15

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 74.01  E-value: 9.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 162 KEVLEVSCGAGGGASYIARNLGpASYTGLDLNPASIDLCRAKHRLPGL----QFVQGDAQNLPFPDESFDAVVNVEASHQ 237
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLARKYG-ANVKGITLSPVQAARANALAAAQGLsdkvSFQVADALNQPFEDGQFDLVWSMESGEH 198

                         90
                 ....*....|....*....
gi 489502777 238 YPDFRGFLAEVARVLRPGG 256
Cdd:PLN02244 199 MPDKRKFVQELARVAAPGG 217
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 165-258 1.30e-13

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 65.85  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  165 LEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCRAKHRLPG------LQFVQGDAQNLPFPdeSFDAVVNVEASHQY 238
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGllnavrVELFQLDLGELDPG--SFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|
gi 489502777  239 PDFRGFLAEVARVLRPGGHF 258
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
164-279 1.47e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 68.10  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 164 VLEVSCGAGggasYIARNLGPASY--TGLDLNPASIDLCRAKHRlpGLQFVQGDAQNLPFPDESFDAVVNVEASHQYPDF 241
Cdd:COG4976   50 VLDLGCGTG----LLGEALRPRGYrlTGVDLSEEMLAKAREKGV--YDRLLVADLADLAEPDGRFDLIVAADVLTYLGDL 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489502777 242 RGFLAEVARVLRPGGHFLYT-----DSRRNPV-VAEWEAALADA 279
Cdd:COG4976  124 AAVFAGVARALKPGGLFIFSvedadGSGRYAHsLDYVRDLLAAA 167
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 164-262 2.32e-13

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: 68.85  E-value: 2.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  164 VLEVSCGAGGGASYIARNLGPASYTGLDLNPAsiDLCRAKHRLPG-LQFVQGDAQNLPFPDESFDAVVNVEASHQYPDFR 242
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALDISAG--MLAQAKTKLSEnVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLS 115

                          90       100
                  ....*....|....*....|
gi 489502777  243 GFLAEVARVLRPGGHFLYTD 262
Cdd:TIGR02072 116 QALSELARVLKPGGLLAFST 135
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
158-259 9.59e-12

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 64.00  E-value: 9.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  158 DLTGKEVLEVSCGAGGGASYIARNLGPA-SYTGLDLNPASIDLCRAKHRLPG---LQFVQGDAQNLPFPDESFDAVVNVE 233
Cdd:pfam01209  40 VKRGNKFLDVAGGTGDWTFGLSDSAGSSgKVVGLDINENMLKEGEKKAKEEGkynIEFLQGNAEELPFEDDSFDIVTISF 119

                          90       100
                  ....*....|....*....|....*.
gi 489502777  234 ASHQYPDFRGFLAEVARVLRPGGHFL 259
Cdd:pfam01209 120 GLRNFPDYLKVLKEAFRVLKPGGRVV 145
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 161-256 3.99e-11

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 61.12  E-value: 3.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGAsyI-ARNLGPASYtGLDLNPASIDLCRA--KH-RLPGLQFVQGDAQNLPFPDESFDAVVnVEA-- 234
Cdd:COG1041   27 GDTVLDPFCGTGTIL--IeAGLLGRRVI-GSDIDPKMVEGAREnlEHyGYEDADVIRGDARDLPLADESVDAIV-TDPpy 102

                         90       100       110
                 ....*....|....*....|....*....|
gi 489502777 235 --SHQYPD------FRGFLAEVARVLRPGG 256
Cdd:COG1041  103 grSSKISGeellelYEKALEEAARVLKPGG 132
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
162-311 5.38e-10

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 58.58  E-value: 5.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777   162 KEVLEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCRAKHRLPGLQ----FVQGDAQNLPFPDEsFDAVVNVEASHQ 237
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQgrirIFYRDSAKDPFPDT-YDLVFGFEVIHH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777   238 YPDFRGFLAEVARVLRPGGHFLYTD--------------SRRNPVVAEWEAALADAPLRTISQRDIGAQAKRGL-DANTA 302
Cdd:smart00828  80 IKDKMDLFSNISRHLKDGGHLVLADfianllsaieheetTSYLVTREEWAELLARNNLRVVEGVDASLEIANFLyDPGFE 159


                   ....*....
gi 489502777   303 RSQEAIGRR 311
Cdd:smart00828 160 DNLERLYQD 168
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 137-261 1.82e-09

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 57.46  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 137 SESDEPNRYCIQLYHQTASQVDLTgkEVLEVSCGAGGGASYiARNLGpASYTGLDLNPASIDlcRAKHRLPGLQFVQGDA 216
Cdd:PRK10258  21 EQHAELQRQSADALLAMLPQRKFT--HVLDAGCGPGWMSRY-WRERG-SQVTALDLSPPMLA--QARQKDAADHYLAGDI 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489502777 217 QNLPFPDESFDAVVNVEASHQYPDFRGFLAEVARVLRPGGHFLYT 261
Cdd:PRK10258  95 ESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFT 139
arsM PRK11873
arsenite methyltransferase;
161-273 2.14e-09

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 57.65  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGPASYT-GLDLNPASIDLCRAKHRLPGL---QFVQGDAQNLPFPDESFDA-----VVN 231
Cdd:PRK11873  78 GETVLDLGSGGGFDCFLAARRVGPTGKViGVDMTPEMLAKARANARKAGYtnvEFRLGEIEALPVADNSVDViisncVIN 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489502777 232 VEashqyPDFRGFLAEVARVLRPGGHFLYTDsrrnpVVAEWE 273
Cdd:PRK11873 158 LS-----PDKERVFKEAFRVLKPGGRFAISD-----VVLRGE 189
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 144-272 2.21e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 55.90  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  144 RYCIQLYHQtASQVDLTGKEVLEVSCGAGGGASYIARNlgPASYTGLDLNPASIDLCRAKHRlpglqFVQGDAQNLPFPD 223
Cdd:pfam13489   7 RLLADLLLR-LLPKLPSPGRVLDFGCGTGIFLRLLRAQ--GFSVTGVDPSPIAIERALLNVR-----FDQFDEQEAAVPA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 489502777  224 ESFDAVVNVEASHQYPDFRGFLAEVARVLRPGGHFLYTDSRRNPVVAEW 272
Cdd:pfam13489  79 GKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL 127
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 158-256 4.27e-09

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 57.21  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 158 DLTGKEVLEVSCGAGGGASY--IARNLGPASYTGLDLNPASIDLCRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEAS 235
Cdd:PLN02490 109 DLSDRNLKVVDVGGGTGFTTlgIVKHVDAKNVTILDQSPHQLAKAKQKEPLKECKIIEGDAEDLPFPTDYADRYVSAGSI 188

                         90       100
                 ....*....|....*....|.
gi 489502777 236 HQYPDFRGFLAEVARVLRPGG 256
Cdd:PLN02490 189 EYWPDPQRGIKEAYRVLKIGG 209
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
181-259 7.39e-09

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 54.10  E-value: 7.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 181 NLGPAS-----YTGLDLNPAS-IDLCrakHRLPGLqfvqgdaqnLPFPDESFDAVVnveASH-----QYPDFRGFLAEVA 249
Cdd:COG4627    8 NIGCGPkrlpgWLNVDIVPAPgVDIV---GDLTDP---------LPFPDNSVDAIY---SSHvlehlDYEEAPLALKECY 72

                         90
                 ....*....|
gi 489502777 250 RVLRPGGHFL 259
Cdd:COG4627   73 RVLKPGGILR 82
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 161-267 8.19e-09

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 56.68  E-value: 8.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGpASYTGLDL--NPASIDLCRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQY 238
Cdd:PLN02336 267 GQKVLDVGCGIGGGDFYMAENFD-VHVVGIDLsvNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHI 345

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502777 239 PD----FRGFLaevaRVLRPGGHFLYTDSRRNP 267
Cdd:PLN02336 346 QDkpalFRSFF----KWLKPGGKVLISDYCRSP 374
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 161-259 6.25e-08

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: 52.11  E-value: 6.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCR---AKHRLPGLQFVQGDAQNlPFPDESFDAVV------- 230
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARanaAANGLENVEVLWSDGLS-GVPDGSFDLILsnppfha 128

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489502777 231 ----NVEASHQypdfrgFLAEVARVLRPGGHFL 259
Cdd:COG2813  129 gravDKEVAHA------LIADAARHLRPGGELW 155
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 156-256 6.07e-07

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 48.74  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  156 QVDLTGKeVLEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCR---AKHRLPGLQFVQGDAQNlPFPDESFDAVV-N 231
Cdd:pfam05175  28 PKDLSGK-VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARenlAANGLENGEVVASDVYS-GVEDGKFDLIIsN 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489502777  232 veashqyPDFR-----------GFLAEVARVLRPGG 256
Cdd:pfam05175 106 -------PPFHaglattynvaqRFIADAKRHLRPGG 134
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 161-258 8.82e-07

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: 49.37  E-value: 8.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCRAKHRLPGL----QFVQGDAQNLP--FPDESFDAVV---- 230
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLedriTVIHGDLKEFAaeLPPGSFDLVVsnpp 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489502777 231 --NVEASHQYPD-------------FRGFLAEVARVLRPGGHF 258
Cdd:COG4123  118 yfKAGSGRKSPDearaiarhedaltLEDLIRAAARLLKPGGRF 160
PRK14968 PRK14968
putative methyltransferase; Provisional
 161-256 1.20e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 48.36  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNlgPASYTGLDLNPASIDL--CRAKH---RLPGLQFVQGDaqnL--PFPDESFDAVV-N- 231
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECakCNAKLnniRNNGVEVIRSD---LfePFRGDKFDVILfNp 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489502777 232 ----VEASHQYPD-----FRG----------FLAEVARVLRPGG 256
Cdd:PRK14968  99 pylpTEEEEEWDDwlnyaLSGgkdgrevidrFLDEVGRYLKPGG 142
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 160-255 2.40e-06

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 48.35  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 160 TGKEVLEVSCGAGGGASYIARNLGP-ASYTGLD------LNPASIDLCRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNV 232
Cdd:PLN02233  73 MGDRVLDLCCGSGDLAFLLSEKVGSdGKVMGLDfsseqlAVAASRQELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMG 152

                         90       100
                 ....*....|....*....|...
gi 489502777 233 EASHQYPDFRGFLAEVARVLRPG 255
Cdd:PLN02233 153 YGLRNVVDRLKAMQEMYRVLKPG 175
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 121-259 2.95e-06

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 47.98  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 121 FFNFGYEEdpPMalplseSDEPNRYCIQLYHQTASQVdltgkevLEVSCGAGGGASYIARNLG---PASYTGLDLNPASI 197
Cdd:PRK11088  61 FLDAGHYQ--PL------RDAVANLLAERLDEKATAL-------LDIGCGEGYYTHALADALPeitTMQLFGLDISKVAI 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489502777 198 DlcRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQypdfrgfLAEVARVLRPGGHFL 259
Cdd:PRK11088 126 K--YAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYAPCK-------AEELARVVKPGGIVI 178
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
162-259 1.11e-05

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 45.59  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 162 KEVLEVSCGAGGGASYIARNLGPASYTGLDLNPASIDLCR-------AKHRLPGLQFVQGDA-QNLPFPDESFDAVVnVE 233
Cdd:COG0421   39 KRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAReyfpllaPAFDDPRLRVVIGDGrAFLREAEESYDVII-VD 117

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489502777 234 AS-HQYPDF----RGFLAEVARVLRPGGHFL 259
Cdd:COG0421  118 LTdPVGPAEglftREFYEDCRRALKPGGVLV 148
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
158-230 1.44e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 1.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489502777 158 DLTGKEVLEVSCGAGG---GASYiarnLGPASYTGLDLNPASIDLCRAKHRLPG--LQFVQGDAQNLPfPDESFDAVV 230
Cdd:COG2263   43 DIEGKTVLDLGCGTGMlaiGAAL----LGAKKVVGVDIDPEALEIARENAERLGvrVDFIRADVTRIP-LGGSVDTVV 115
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
192-261 2.06e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 45.67  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 192 LNPASIDLcrakhRLPGLQFVQGDAQNL--PFPDESFDAVVnveasHQYPDFRG--------FLAEVARVLRPGGH-FLY 260
Cdd:COG2521  173 LNPWSREL-----ANERIKIILGDASEVikTFPDESFDAII-----HDPPRFSLagelysleFYRELYRVLKPGGRlFHY 242


                 .
gi 489502777 261 T 261
Cdd:COG2521  243 T 243
DUF938 pfam06080
Protein of unknown function (DUF938); This family consists of several hypothetical proteins ...
 155-297 6.37e-05

Protein of unknown function (DUF938); This family consists of several hypothetical proteins from both prokaryotes and eukaryotes. The function of this family is unknown.


Pssm-ID: 253548  Cd Length: 201  Bit Score: 43.21  E-value: 6.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  155 SQVDLTGKEVLEVSCGAGGGASYIARNLGPASYTGLDLNP---ASIDLCRAKHRLPGLQF-VQGDAQNLPFP-----DES 225
Cdd:pfam06080  20 SYFAKTTERVLEIASGTGQHAVFFAPLLPNLTWQPSDPDPnlrGSIAAWADQQGLRNLRPpLHLDVTRPPWPveapaPAS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  226 FDAVVNVEASH--QYPDFRGFLAEVARVLRPGGH-FLYTDSRRNPVVAEWEAALADAPLRtisQRD-----------IGA 291
Cdd:pfam06080 100 YDAIFSINMIHisPWSCVEGLFRGAGRLLPPGGVlYIYGPYNQDGELTSDSNRDFDRSLR---QRDpewgirdiedvIAL 176


                  ....*.
gi 489502777  292 QAKRGL 297
Cdd:pfam06080 177 AAAQGL 182
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 165-259 1.50e-04

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 40.37  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  165 LEVSCGAGGGASYIARNL---GPASYTGLDLNPASIDLCR--AKHRLPG-LQFVQGDAQNL--PFPDESFDaVVNVEASH 236
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALrdnGLGRLTAVDPDPGAEEAGAllRKAGLDDrVRLIVGDSREAlpSLADGPID-LLFIDGDH 79

                          90       100
                  ....*....|....*....|...
gi 489502777  237 QYPDFRGFLAEVARVLRPGGHFL 259
Cdd:pfam13578  80 TYEAVLNDLELWLPRLAPGGVIL 102
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 161-253 1.66e-03

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 38.98  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  161 GKEVLEVSCGAGGGASYIARNLGPASYtGLDLNPASIDLCRAKhrlpGLQFVQGDAQN--LPFPDESFDAVV---NVEAS 235
Cdd:pfam07021  14 GSRVLDLGCGDGTLLYLLKEEKGVDGY-GIELDAAGVAECVAK----GLYVIQGDLDEglEHFPDKSFDYVIlsqTLQAT 88

                          90
                  ....*....|....*...
gi 489502777  236 HqYPdfRGFLAEVARVLR 253
Cdd:pfam07021  89 R-NP--REVLDEMLRIGR 103
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 161-259 2.64e-03

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 38.99  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 161 GKEVLEVSCGAGGGASYIARNLGP-ASYTGLDLNPASIDLCRA---KHRLPG-LQFVQGDAQNlPFPDESFDAVV----- 230
Cdd:COG2519   92 GARVLEAGTGSGALTLALARAVGPeGKVYSYERREDFAEIARKnleRFGLPDnVELKLGDIRE-GIDEGDVDAVFldmpd 170

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489502777 231 --NVeashqypdfrgfLAEVARVLRPGGHFL 259
Cdd:COG2519  171 pwEA------------LEAVAKALKPGGVLV 189
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 161-279 3.94e-03

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 37.65  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  161 GKEVLEVSCGAGGGASYIARNLGPASYTGLDLNPASID--LCRA-KHRLPGLQFVQGDAQN-LP--FPDESFDAVvnvea 234
Cdd:pfam02390   2 APVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAkaLKKIdALGLQNLRILCGNALDvLPnyFPPGSLQKI----- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777  235 SHQYPD----FR---------GFLAEVARVLRPGGhFLY--TDsrrNPVVAEWEAALADA 279
Cdd:pfam02390  77 FINFPDpwpkKRhhkrrllqpEFLKEYARVLKPGG-VLHlaTD---VEEYAEEMLKHLAE 132
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
210-258 5.74e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 37.59  E-value: 5.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502777 210 QFVQGDA-QNLP-FPDESFDAVV-------------------NVEASHQYPDF-RGFLAEVARVLRPGGHF 258
Cdd:COG0863    1 RLICGDClEVLKeLPDESVDLIVtdppynlgkkyglgrreigNELSFEEYLEFlREWLAECYRVLKPGGSL 71
PRK06202 PRK06202
hypothetical protein; Provisional
 164-268 6.82e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 37.67  E-value: 6.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502777 164 VLEVSCGAGGGASYIA----RNLGPASYTGLDLNPASIDLCRAKHRLPGLQFVQGDAQNLPFPDESFDAVVNVEASHQY- 238
Cdd:PRK06202  64 LLDIGCGGGDLAIDLArwarRDGLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAEGERFDVVTSNHFLHHLd 143

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489502777 239 -PDFRGFLAEVARVLRpgGHFLYTDSRRNPV 268
Cdd:PRK06202 144 dAEVVRLLADSAALAR--RLVLHNDLIRSRL 172
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 189-255 7.89e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 36.59  E-value: 7.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502777 189 GLDLNPASIDLCRAKHRLPG------LQFVQGDAQNLPFPDESFDAVVNVEASHQYPDFRGFLAEVARVLRPG 255
Cdd:PLN02232   2 GLDFSSEQLAVAATRQSLKArscykcIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPG 74
 
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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