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Conserved domains on  [gi|1490190182|gb|RKY67043|]
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MAG: ubiquinone biosynthesis protein UbiE [Candidatus Latescibacterota bacterium]

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]; ...
 22-137 1.95e-38

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: 130.50  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  22 RAVDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPE----VPLVRGDATSLP 97
Cdd:COG2226     4 VAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490190182  98 FKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:COG2226    83 FPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 22-137 1.95e-38

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: 130.50  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  22 RAVDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPE----VPLVRGDATSLP 97
Cdd:COG2226     4 VAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490190182  98 FKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:COG2226    83 FPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 44-133 7.07e-34

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 116.89  E-value: 7.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  44 VLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARL----PEVPLVRGDATSLPFKEGSFDVVVAVTVLEFVPEP- 118
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPd 80

                          90
                  ....*....|....*.
gi 1490190182 119 -KEVLDEMWRCVRPGG 133
Cdd:pfam13649  81 lEAALREIARVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 29-137 1.74e-30

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 112.55  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  29 RRAFLRLLEPRVGERVLEVGCGTGHWT-KWFRE-GLGMRVVGLDLSEGMLAVARARL------PEVPLVRGDATSLPFKE 100
Cdd:PRK00216   40 RRKTIKWLGVRPGDKVLDLACGTGDLAiALAKAvGKTGEVVGLDFSEGMLAVGREKLrdlglsGNVEFVQGDAEALPFPD 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490190182 101 GSFDvvvAVTV---LEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PRK00216  120 NSFD---AVTIafgLRNVPDIDKALREMYRVLKPGGRLVI 156
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 2-137 2.99e-25

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: 98.49  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182   2 ENIWDEVSVRYeDWYETPLGRAVDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGMR--VVGLDLSEGMLAVA 79
Cdd:TIGR01934   2 QEMFDRIAPKY-DLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRgkVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490190182  80 RARLPE---VPLVRGDATSLPFKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:TIGR01934  81 KKKSELplnIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVI 141
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-141 3.78e-17

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: 74.00  E-value: 3.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVAR-----ARLPEVPLVRGDATSLPFKE-GSFDVVVAVTVLEFVP 116
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARkaaaaLLADNVEVLKGDAEELPPEAdESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....*.
gi 1490190182 117 E-PKEVLDEMWRCVRPGGRMAVGALH 141
Cdd:cd02440    81 EdLARFLEEARRLLKPGGVLVLTLVL 106
rADc smart00650
Ribosomal RNA adenine dimethylases;
30-108 4.16e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.50  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182   30 RAFLRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEVP---LVRGDATSLPFKEGSFDVV 106
Cdd:smart00650   3 DKIVRAANLRPGDTVLEIGPGKGALTEELLE-RAKRVTAIEIDPRLAPRLREKFAAADnltVIHGDALKFDLPKLQPYKV 81


                   ..
gi 1490190182  107 VA 108
Cdd:smart00650  82 VG 83
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 22-137 1.95e-38

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: 130.50  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  22 RAVDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPE----VPLVRGDATSLP 97
Cdd:COG2226     4 VAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490190182  98 FKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:COG2226    83 FPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 44-133 7.07e-34

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 116.89  E-value: 7.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  44 VLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARL----PEVPLVRGDATSLPFKEGSFDVVVAVTVLEFVPEP- 118
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPd 80

                          90
                  ....*....|....*.
gi 1490190182 119 -KEVLDEMWRCVRPGG 133
Cdd:pfam13649  81 lEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 29-137 8.04e-33

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: 115.50  E-value: 8.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  29 RRAFLRLLEPRV--GERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEVPL--VRGDATSLPFKEGSFD 104
Cdd:COG2227    11 DRRLAALLARLLpaGGRVLDVGCGTGRLALALAR-RGADVTGVDISPEALEIARERAAELNVdfVQGDLEDLPLEDGSFD 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1490190182 105 VVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:COG2227    90 LVICSEVLEHLPDPAALLRELARLLKPGGLLLL 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-137 3.11e-32

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 112.76  E-value: 3.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  45 LEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEVPL--VRGDATSLPFKEGSFDVVVAVTVLEFVPEPKEVL 122
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLtfVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....*
gi 1490190182 123 DEMWRCVRPGGRMAV 137
Cdd:pfam08241  80 REIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
1-136 6.35e-31

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 112.01  E-value: 6.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182   1 MENIWDEVSVRYEDWYETPLGRAVDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVAR 80
Cdd:COG4976     7 VEALFDQYADSYDAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRP-RGYRLTGVDLSEEMLAKAR 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490190182  81 ARLPEVPLVRGDATSLPFKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMA 136
Cdd:COG4976    86 EKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
41-137 8.06e-31

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 109.14  E-value: 8.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  41 GERVLEVGCGTGHWTKWFREGL-GMRVVGLDLSEGMLAVARARLPEVPLVRGDATSLPFkEGSFDVVVAVTVLEFVPEPK 119
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDP-PEPFDLVVSNAALHWLPDHA 80

                          90
                  ....*....|....*...
gi 1490190182 120 EVLDEMWRCVRPGGRMAV 137
Cdd:COG4106    81 ALLARLAAALAPGGVLAV 98
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 29-137 1.74e-30

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 112.55  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  29 RRAFLRLLEPRVGERVLEVGCGTGHWT-KWFRE-GLGMRVVGLDLSEGMLAVARARL------PEVPLVRGDATSLPFKE 100
Cdd:PRK00216   40 RRKTIKWLGVRPGDKVLDLACGTGDLAiALAKAvGKTGEVVGLDFSEGMLAVGREKLrdlglsGNVEFVQGDAEALPFPD 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490190182 101 GSFDvvvAVTV---LEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PRK00216  120 NSFD---AVTIafgLRNVPDIDKALREMYRVLKPGGRLVI 156
PRK08317 PRK08317
hypothetical protein; Provisional
 29-137 2.59e-30

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 112.34  E-value: 2.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  29 RRAFLRLLEPRVGERVLEVGCGTGHWTKWF--REGLGMRVVGLDLSEGMLAVARAR----LPEVPLVRGDATSLPFKEGS 102
Cdd:PRK08317    8 RARTFELLAVQPGDRVLDVGCGPGNDARELarRVGPEGRVVGIDRSEAMLALAKERaaglGPNVEFVRGDADGLPFPDGS 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1490190182 103 FDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PRK08317   88 FDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVV 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 2-137 5.25e-26

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 98.85  E-value: 5.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182   2 ENIWDEvSVRYEDWYETPLGRAVDEAER---RAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAV 78
Cdd:COG2230    11 RLFLDP-TMTYSCAYFEDPDDTLEEAQEaklDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEY 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490190182  79 ARARLPE------VPLVRGDATSLPFkEGSFDVVVAVTVLEFVPEPK--EVLDEMWRCVRPGGRMAV 137
Cdd:COG2230    90 ARERAAEagladrVEVRLADYRDLPA-DGQFDAIVSIGMFEHVGPENypAYFAKVARLLKPGGRLLL 155
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 2-137 2.99e-25

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: 98.49  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182   2 ENIWDEVSVRYeDWYETPLGRAVDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGMR--VVGLDLSEGMLAVA 79
Cdd:TIGR01934   2 QEMFDRIAPKY-DLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRgkVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490190182  80 RARLPE---VPLVRGDATSLPFKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:TIGR01934  81 KKKSELplnIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVI 141
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 12-140 3.41e-22

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 89.98  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  12 YEDWYETPLGRAVDeaerRAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARLPE-----V 86
Cdd:COG0500     2 WDSYYSDELLPGLA----ALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKaglgnV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1490190182  87 PLVRGDAT-SLPFKEGSFDVVVAVTVLEFVP--EPKEVLDEMWRCVRPGGRMAVGAL 140
Cdd:COG0500    78 EFLVADLAeLDPLPAESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLLSAS 134
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-134 2.69e-20

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 82.03  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  45 LEVGCGTGHWTKWFREGL-GMRVVGLDLSEGMLAVARARLPE-----VPLVRGDATSLPF-KEGSFDVVVAVTVLEFVPE 117
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAAlgllnAVRVELFQLDLGElDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*..
gi 1490190182 118 PKEVLDEMWRCVRPGGR 134
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGV 97
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 21-144 4.71e-19

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 82.88  E-value: 4.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  21 GRAV------DEAERR---AFLRLLEPRVGERVLEVGCGTGHWTKWFREGlGMRVVGLDLSEGMLAVARARLPEVPLVRG 91
Cdd:PRK10258   14 GRAAahyeqhAELQRQsadALLAMLPQRKFTHVLDAGCGPGWMSRYWRER-GSQVTALDLSPPMLAQARQKDAADHYLAG 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1490190182  92 DATSLPFKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAVGALHEGS 144
Cdd:PRK10258   93 DIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGS 145
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
29-137 3.84e-18

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 79.79  E-value: 3.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  29 RRAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGMR--VVGLDLSEGMLAVARARLPE-----VPLVRGDATSLPFKEG 101
Cdd:pfam01209  31 KDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSgkVVGLDINENMLKEGEKKAKEegkynIEFLQGNAEELPFEDD 110

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490190182 102 SFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:pfam01209 111 SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVC 146
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 31-142 1.75e-17

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: 78.10  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  31 AFLRLLEPRVGERVLEVGCGTGHWTK-WFREGLGMRVVGLDLSEGMLAVARARLPE-VPLVRGDATSLPFKEGSFDVVVA 108
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRaLLKRFPQAEFIALDISAGMLAQAKTKLSEnVQFICGDAEKLPLEDSSFDLIVS 104

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490190182 109 VTVLEFVPEPKEVLDEMWRCVRPGGRMAV-----GALHE 142
Cdd:TIGR02072 105 NLALQWCDDLSQALSELARVLKPGGLLAFstfgpGTLHE 143
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-141 3.78e-17

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: 74.00  E-value: 3.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVAR-----ARLPEVPLVRGDATSLPFKE-GSFDVVVAVTVLEFVP 116
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARkaaaaLLADNVEVLKGDAEELPPEAdESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....*.
gi 1490190182 117 E-PKEVLDEMWRCVRPGGRMAVGALH 141
Cdd:cd02440    81 EdLARFLEEARRLLKPGGVLVLTLVL 106
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 41-137 4.48e-17

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 75.15  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  41 GERVLEVGCGTGHWTKWFREGLGM--RVVGLDLSEGMLAVARAR-----LPEVPLVRGDATSLP--FKEGSFDVVVAVTV 111
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEELGPnaEVVGIDISEEAIEKARENaqklgFDNVEFEQGDIEELPelLEDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|....*.
gi 1490190182 112 LEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLII 109
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 22-176 1.90e-16

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 73.62  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  22 RAVDEAERRAFLRLL-EPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEVPLVRGDATslpFKE 100
Cdd:pfam13489   3 HQRERLLADLLLRLLpKLPSPGRVLDFGCGTGIFLRLLRA-QGFSVTGVDPSPIAIERALLNVRFDQFDEQEAA---VPA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182 101 GSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMaVGALHEGSPFARRRRTSGTVLS----HARLFGYDELKELLGHYG 176
Cdd:pfam13489  79 GKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLL-LLSTPLASDEADRLLLEWPYLRprngHISLFSARSLKRLLEEAG 157
arsM PRK11873
arsenite methyltransferase;
41-137 2.50e-13

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 67.28  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  41 GERVLEVGCGTGhwtkwF-------REGLGMRVVGLDLSEGMLAVARAR-----LPEVPLVRGDATSLPFKEGSFDVVVA 108
Cdd:PRK11873   78 GETVLDLGSGGG-----FdcflaarRVGPTGKVIGVDMTPEMLAKARANarkagYTNVEFRLGEIEALPVADNSVDVIIS 152

                          90       100
                  ....*....|....*....|....*....
gi 1490190182 109 VTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PRK11873  153 NCVINLSPDKERVFKEAFRVLKPGGRFAI 181
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 30-137 3.01e-13

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: 65.36  E-value: 3.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEPRVGERVLEVGCGTGhwtkwfreG-------LGMRVVGLDLSEGMLAVARARL-----PEVPLVRGDATSLP 97
Cdd:COG1041    16 RALVNLAGAKEGDTVLDPFCGTG--------TilieaglLGRRVIGSDIDPKMVEGARENLehygyEDADVIRGDARDLP 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1490190182  98 FKEGSFDVVV------------AVTVLEFVpepKEVLDEMWRCVRPGGRMAV 137
Cdd:COG1041    88 LADESVDAIVtdppygrsskisGEELLELY---EKALEEAARVLKPGGRVVI 136
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 41-135 2.41e-12

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 63.85  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  41 GERVLEVGCGTGHWTkwfrEGL---GMRVVGLDLSEGMLAVARARLPEVPL-VRGDATSL----PFKEGSFDVVVAVTVL 112
Cdd:TIGR01983  47 GLRVLDVGCGGGLLS----EPLarlGANVTGIDASEENIEVAKLHAKKDPLqIDYRCTTVedlaEKKAGSFDVVTCMEVL 122

                          90       100
                  ....*....|....*....|...
gi 1490190182 113 EFVPEPKEVLDEMWRCVRPGGRM 135
Cdd:TIGR01983 123 EHVPDPQAFIRACAQLLKPGGIL 145
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 27-130 1.18e-10

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: 58.62  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  27 AERRAFLRLLEPrvGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARlpEVPLVRGDA-TSLP-FKEGSFD 104
Cdd:pfam07021   2 ADFRYILEWIPP--GSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAK--GLYVIQGDLdEGLEhFPDKSFD 77

                          90       100
                  ....*....|....*....|....*.
gi 1490190182 105 VVVAVTVLEFVPEPKEVLDEMWRCVR 130
Cdd:pfam07021  78 YVILSQTLQATRNPREVLDEMLRIGR 103
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 35-137 2.36e-10

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 58.80  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  35 LLEPRvgeRVLEVGCGTGHWTKWFREGLGM-RVVGLDLSEGMLAVARARLPEVPLVRGDATSLPFKEGSfDVVVAVTVLE 113
Cdd:PRK01683   29 LENPR---YVVDLGCGPGNSTELLVERWPAaRITGIDSSPAMLAEARSRLPDCQFVEADIASWQPPQAL-DLIFANASLQ 104

                          90       100
                  ....*....|....*....|....
gi 1490190182 114 FVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PRK01683  105 WLPDHLELFPRLVSLLAPGGVLAV 128
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 39-137 1.10e-09

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 56.82  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  39 RVGERVLEVGCGTGHWTKWFREGLGM--RVVGLDLSEGMLAVARARLP--------EVPLVRGDATSLPFKEGSFDVVVA 108
Cdd:PLN02233   72 KMGDRVLDLCCGSGDLAFLLSEKVGSdgKVMGLDFSSEQLAVAASRQElkakscykNIEWIEGDATDLPFDDCYFDAITM 151

                          90       100
                  ....*....|....*....|....*....
gi 1490190182 109 VTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PLN02233  152 GYGLRNVVDRLKAMQEMYRVLKPGSRVSI 180
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 43-148 1.26e-08

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 54.13  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTkwfregLGM-------RVVGLDLSEGMLAVARARLP--EVPLVRGDATSLPFKEGSFDVVVAVTVLE 113
Cdd:PLN02490  116 KVVDVGGGTGFTT------LGIvkhvdakNVTILDQSPHQLAKAKQKEPlkECKIIEGDAEDLPFPTDYADRYVSAGSIE 189

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490190182 114 FVPEPKEVLDEMWRCVRPGGRMA-VGALHEGSPFAR 148
Cdd:PLN02490  190 YWPDPQRGIKEAYRVLKIGGKAClIGPVHPTFWLSR 225
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 41-137 1.50e-08

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: 53.62  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  41 GERVLEVGCGTGHWTKWFREGLGM--RVVGLDLSEGMLAVARARL------PEVPLVRGDATSlPFKEGSFDVVVAvtvl 112
Cdd:COG2519    92 GARVLEAGTGSGALTLALARAVGPegKVYSYERREDFAEIARKNLerfglpDNVELKLGDIRE-GIDEGDVDAVFL---- 166

                          90       100
                  ....*....|....*....|....*
gi 1490190182 113 eFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:COG2519   167 -DMPDPWEALEAVAKALKPGGVLVA 190
PLN02244 PLN02244
tocopherol O-methyltransferase
 22-134 1.66e-08

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 53.98  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  22 RAVDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARLPE------VPLVRGDATS 95
Cdd:PLN02244  100 RMIEESLAWAGVPDDDEKRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAqglsdkVSFQVADALN 179

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490190182  96 LPFKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGR 134
Cdd:PLN02244  180 QPFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGR 218
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 33-139 2.25e-08

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 50.79  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  33 LRLLEPRVGERVLEVGCGTG----HWTKWFREGlgmRVVGLDLSEG-----MLAVARARLPEVPLVRGDATSLPfkEGSF 103
Cdd:TIGR02469  12 LAKLRLRPGDVLWDIGAGTGsvtiEAARLVPNG---RVYAIERNPEaldliERNLRRFGVSNIVIVEGDAPEAP--EALL 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1490190182 104 DVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAVGA 139
Cdd:TIGR02469  87 PDPDAVFVGGSGGLLQEILEAVERRLRPGGRIVLNA 122
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 33-137 5.52e-08

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 51.24  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  33 LRLLEPRVGERVLEVGCGTG-------HwtkwfregLGMRVVGLDLSEGMLAVARARLPE-----VPLVRGDATSLPFKE 100
Cdd:COG2518    59 LEALDLKPGDRVLEIGTGSGyqaavlaR--------LAGRVYSVERDPELAERARERLAAlgydnVTVRVGDGALGWPEH 130

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490190182 101 GSFDVVVaVTV-LEFVPEPkevldeMWRCVRPGGRMAV 137
Cdd:COG2518   131 APFDRII-VTAaAPEVPEA------LLEQLAPGGRLVA 161
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
43-133 1.91e-07

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 50.35  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEvplvRGDATSLPFK-----------EGSFDVVVAVTV 111
Cdd:PRK11036   47 RVLDAGGGEGQTAIKLAE-LGHQVILCDLSAEMIQRAKQAAEA----KGVSDNMQFIhcaaqdiaqhlETPVDLILFHAV 121

                          90       100
                  ....*....|....*....|..
gi 1490190182 112 LEFVPEPKEVLDEMWRCVRPGG 133
Cdd:PRK11036  122 LEWVADPKSVLQTLWSVLRPGG 143
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
41-107 2.32e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 2.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490190182  41 GERVLEVGCGTGhwtkwfREGLGM------RVVGLDLSEGMLAVARARLPE----VPLVRGDATSLPFkEGSFDVVV 107
Cdd:COG2263    46 GKTVLDLGCGTG------MLAIGAallgakKVVGVDIDPEALEIARENAERlgvrVDFIRADVTRIPL-GGSVDTVV 115
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 30-166 2.39e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 50.52  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVA--RA--RLPEVPLVRGDATSLPFKEGSFDV 105
Cdd:PLN02336  256 KEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFAleRAigRKCSVEFEVADCTKKTYPDNSFDV 335

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490190182 106 VVAV-TVLEFVPEPKeVLDEMWRCVRPGGRMAVgalhegSPFARRRRT-SGTVLSHARLFGYD 166
Cdd:PLN02336  336 IYSRdTILHIQDKPA-LFRSFFKWLKPGGKVLI------SDYCRSPGTpSPEFAEYIKQRGYD 391
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 30-133 2.50e-07

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 49.03  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEPRvgeRVLEVGCGTGHWTKWFREGL--GMRVVGLDLSEGMLAVARARLPEVP------LVRGDAT-SLP-FK 99
Cdd:COG4122     9 YLLARLLGAK---RILEIGTGTGYSTLWLARALpdDGRLTTIEIDPERAAIARENFARAGladrirLILGDALeVLPrLA 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490190182 100 EGSFDVVvavtvleFV----PEPKEVLDEMWRCVRPGG 133
Cdd:COG4122    86 DGPFDLV-------FIdadkSNYPDYLELALPLLRPGG 116
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 41-112 9.38e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 47.91  E-value: 9.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  41 GERVLEVGCGTGHWT----KwfregLGMRVVGLDLSEGMLAVARARLPEVPLVR------GDATSLpfkEGSFDVVVAVT 110
Cdd:PRK07580   64 GLRILDAGCGVGSLSiplaR-----RGAKVVASDISPQMVEEARERAPEAGLAGnitfevGDLESL---LGRFDTVVCLD 135


                  ..
gi 1490190182 111 VL 112
Cdd:PRK07580  136 VL 137
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
43-135 9.85e-07

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 47.17  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTKWfreglgmrvVGLDLSEGmlavararlPEVPLVRGDATSLPFKEGSFDVVVAVTVLE--FVPEPKE 120
Cdd:COG4627     5 LKLNIGCGPKRLPGW---------LNVDIVPA---------PGVDIVGDLTDPLPFPDNSVDAIYSSHVLEhlDYEEAPL 66

                          90
                  ....*....|....*
gi 1490190182 121 VLDEMWRCVRPGGRM 135
Cdd:COG4627    67 ALKECYRVLKPGGIL 81
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 30-137 3.47e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 46.61  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEpRVGE----RVLEVGCGTGHWTKWFREGL-GMRVVGLDLSEGMLAVARARLpeVPLVRGDATSLPFKEgSFD 104
Cdd:PRK14103   16 RPFYDLLA-RVGAerarRVVDLGCGPGNLTRYLARRWpGAVIEALDSSPEMVAAARERG--VDARTGDVRDWKPKP-DTD 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1490190182 105 VVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PRK14103   92 VVVSNAALQWVPEHADLLVRWVDELAPGSWIAV 124
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 33-172 4.16e-06

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 46.64  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  33 LRLLEPRVGERVLEVGCGT-GH----WTKWfregLGMRVVGLDLSEGMLAVARA----------RLPEVPLVRGdatslp 97
Cdd:COG1064   155 LRRAGVGPGDRVAVIGAGGlGHlavqIAKA----LGAEVIAVDRSPEKLELARElgadhvvnssDEDPVEAVRE------ 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  98 fkEGSFDVVvavtvLEFVPEPkEVLDEMWRCVRPGGRMAVGALHEGSP-------FARRRRTSGtvlSHArlFGYDELKE 170
Cdd:COG1064   225 --LTGADVV-----IDTVGAP-ATVNAALALLRRGGRLVLVGLPGGPIplppfdlILKERSIRG---SLI--GTRADLQE 291


                  ..
gi 1490190182 171 LL 172
Cdd:COG1064   292 ML 293
PRK05785 PRK05785
hypothetical protein; Provisional
 43-130 6.71e-06

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 45.45  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLavaRARLPEVPLVRGDATSLPFKEGSFDVVVAVTVLEFVPEPKEVL 122
Cdd:PRK05785   54 KVLDVAAGKGELSYHFKKVFKYYVVALDYAENML---KMNLVADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVI 130


                  ....*...
gi 1490190182 123 DEMWRCVR 130
Cdd:PRK05785  131 AEFTRVSR 138
PRK14968 PRK14968
putative methyltransferase; Provisional
 33-107 8.15e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  33 LRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEgmLAVARA---------RLPEVPLVRGDATSlPFKEGSF 103
Cdd:PRK14968   16 AENAVDKKGDRVLEVGTGSGIVAIVAAK-NGKKVVGVDINP--YAVECAkcnaklnniRNNGVEVIRSDLFE-PFRGDKF 91


                  ....
gi 1490190182 104 DVVV 107
Cdd:PRK14968   92 DVIL 95
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 24-123 1.46e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 44.76  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  24 VDEAerrafLRLLEPRVGERVLEVGCGTG--------HWTKWfreglgmRVVGLDLSEGMLAVAR---ARL---PEVPLV 89
Cdd:COG2890   101 VELA-----LALLPAGAPPRVLDLGTGSGaialalakERPDA-------RVTAVDISPDALAVARrnaERLgleDRVRFL 168

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1490190182  90 RGDATSLPFKEGSFDVVVA----VTVLEFVPEPKEVLD 123
Cdd:COG2890   169 QGDLFEPLPGDGRFDLIVSnppyIPEDEIALLPPEVRD 206
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 33-154 1.51e-05

Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 45.00  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  33 LRLLEPRVGERVLEVGCG-TGHWTKWFREGLGMRVVGLDLSEGMLAVARARLPEVPLVRGDATSLPFKEGSFDVVVAVTV 111
Cdd:cd08245   155 LRDAGPRPGERVAVLGIGgLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQAAAGGADVILVTVV 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490190182 112 LEfvpepkEVLDEMWRCVRPGGRMAVGALHEGSPF--------ARRRRTSG 154
Cdd:cd08245   235 SG------AAAEAALGGLRRGGRIVLVGLPESPPFspdifpliMKRQSIAG 279
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 67-137 1.79e-05

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 43.52  E-value: 1.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490190182  67 VGLDLSEGMLAVARAR--------LPEVPLVRGDATSLPFKEGSFDVVVAVTVLEFVPEPKEVLDEMWRCVRPGGRMAV 137
Cdd:PLN02232    1 MGLDFSSEQLAVAATRqslkarscYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSI 79
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 24-104 2.72e-05

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 43.76  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  24 VDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEVP---LVRGDATSLPFKE 100
Cdd:TIGR00755  13 VDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLK-RAKKVTAIEIDPRLAERLRKLLSLYNnleIIEGDALKFDLNE 91


                  ....
gi 1490190182 101 GSFD 104
Cdd:TIGR00755  92 LAKD 95
rADc smart00650
Ribosomal RNA adenine dimethylases;
30-108 4.16e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.50  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182   30 RAFLRLLEPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEVP---LVRGDATSLPFKEGSFDVV 106
Cdd:smart00650   3 DKIVRAANLRPGDTVLEIGPGKGALTEELLE-RAKRVTAIEIDPRLAPRLREKFAAADnltVIHGDALKFDLPKLQPYKV 81


                   ..
gi 1490190182  107 VA 108
Cdd:smart00650  82 VG 83
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 30-135 4.53e-05

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: 42.87  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEPRVGERVLEVGCGTG---HWTKwfREGLGMRVVGLDLSEgmLAVARAR-------LPEVPLVRGDATSlPFK 99
Cdd:COG2813    39 RLLLEHLPEPLGGRVLDLGCGYGvigLALA--KRNPEARVTLVDVNA--RAVELARanaaangLENVEVLWSDGLS-GVP 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1490190182 100 EGSFDVVV---------AVTvlefvpepKEVLDEM----WRCVRPGGRM 135
Cdd:COG2813   114 DGSFDLILsnppfhagrAVD--------KEVAHALiadaARHLRPGGEL 154
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 30-161 6.18e-05

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 42.34  E-value: 6.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEPRVGERVLEVGCGTG--------HWTK----WFREGLGMRVVGLDLSEGMLAVAR--ARLPEVP----LVRG 91
Cdd:pfam01170  18 AAMVNLAGWKPGDPLLDPMCGSGtilieaalMGANiapgKFDARVRAPLYGSDIDRRMVQGARlnAENAGVGdlieFVQA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  92 DATSLPFKEGSFDVVV-----------AVTVLEFVPepkEVLDEMWRCVRPGGRmAVGALHEGSPFARRRRTSGTVLSHA 160
Cdd:pfam01170  98 DAADLPLLEGSVDVIVtnppygirlgsKGALEALYP---EFLREAKRVLRGGGW-LVLLTAENKDFEKAARERAWRKKKE 173


                  .
gi 1490190182 161 R 161
Cdd:pfam01170 174 F 174
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
43-147 6.63e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 42.41  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTKWFrEGLGMRVVGLDLSEGMLA-----VARARLPEVPLVRGDATSLPFkEGSFDVVVAVTVLEFVpE 117
Cdd:PRK11207   33 KTLDLGCGNGRNSLYL-AANGFDVTAWDKNPMSIAnleriKAAENLDNLHTAVVDLNNLTF-DGEYDFILSTVVLMFL-E 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1490190182 118 PKEV---LDEMWRCVRPGG-RMAVGAL-------HEGSPFA 147
Cdd:PRK11207  110 AKTIpglIANMQRCTKPGGyNLIVAAMdtadypcTVGFPFA 150
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 30-133 7.13e-05

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: 42.19  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLE-------PRVGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARlPEVPLVRGDATSL------ 96
Cdd:pfam01728   4 RAAYKLLEidekfglLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQLWKPRND-PGVTFIQGDIRDPetldll 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1490190182  97 -PFKEGSFDVVVA-----VTVLEFVPEP------KEVLDEMWRCVRPGG 133
Cdd:pfam01728  83 eELLGRKVDLVLSdgspfISGNKVLDHLrsldlvKAALEVALELLRKGG 131
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
41-108 7.59e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 42.58  E-value: 7.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490190182  41 GERVLEVGCGTGHWTKwFREGLGMRVVGLDLSEGMLAVARARLPEVP---LVRGDATSLPFKEgsFDVVVA 108
Cdd:PRK14896   30 GDPVLEIGPGKGALTD-ELAKRAKKVYAIELDPRLAEFLRDDEIAAGnveIIEGDALKVDLPE--FNKVVS 97
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
34-137 8.08e-05

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 42.48  E-value: 8.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  34 RLLEPRVGERVLEVGCGTG------------HWTKWFREglgMRVVGLDLSEGMLAVARARL-----PEVPLVRGDA-TS 95
Cdd:COG0286    37 ELLDPKPGETVYDPACGSGgflveaaeylkeHGGDERKK---LSLYGQEINPTTYRLAKMNLllhgiGDPNIELGDTlSN 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490190182  96 LPFKEGSFDVVVA-----------------VTVLEFVPEPK---EV--LDEMWRCVRPGGRMAV 137
Cdd:COG0286   114 DGDELEKFDVVLAnppfggkwkkeelkddlLGRFGYGLPPKsnaDLlfLQHILSLLKPGGRAAV 177
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 24-108 1.02e-04

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.46  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  24 VDEAerrafLRLLEPRVGERVLEVGCGTG--------HWTKWfreglgmRVVGLDLSEGMLAVAR---ARLPE--VPLVR 90
Cdd:PRK09328   97 VEWA-----LEALLLKEPLRVLDLGTGSGaialalakERPDA-------EVTAVDISPEALAVARrnaKHGLGarVEFLQ 164

                          90
                  ....*....|....*...
gi 1490190182  91 GDATSlPFKEGSFDVVVA 108
Cdd:PRK09328  165 GDWFE-PLPGGRFDLIVS 181
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 32-174 1.06e-04

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 42.03  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  32 FLRLLEPRVGERVLEVGCGTGHWTKWFREGlGMRVVGLDLSEgmLAVARA-------------------RLPEVPLVRGD 92
Cdd:pfam05724  29 HWDALKLPPGLRVLVPLCGKALDMVWLAEQ-GHFVVGVEISE--LAVEKFfaeaglsppitelsgfkeySSGNISLYCGD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  93 ATSLPFKE-GSFDVV---VAVTVLEfvPEPKE-VLDEMWRCVRPGGR------MAVGALHEGSPF----ARRRRTSGTVL 157
Cdd:pfam05724 106 FFTLPREElGKFDLIydrAALCALP--PEMRPrYAKQMYELLPPGGRgllitlDYPQTDHEGPPFsvpaAELEALFGGGW 183

                         170
                  ....*....|....*..
gi 1490190182 158 SHARLFGYDELKELLGH 174
Cdd:pfam05724 184 KVAELEREDALVPEPRF 200
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
31-137 1.22e-04

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 41.58  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  31 AFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGM--RVVGLDLSEGMLAVARARLPevplvRGDATSLPFKEGS------ 102
Cdd:pfam01135  64 MMLELLELKPGMRVLEIGSGSGYLTACFARMVGEvgRVVSIEHIPELVEIARRNLE-----KLGLENVIVVVGDgrqgwp 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1490190182 103 ----FDvvvAVTVLEFVPE-PKEVLDEMwrcvRPGGRMAV 137
Cdd:pfam01135 139 efapYD---AIHVGAAAPEiPEALIDQL----KEGGRLVI 171
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 25-144 1.25e-04

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 41.93  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  25 DEAERRAFLRLLEP---RVGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARLPEVPLVRG------DATS 95
Cdd:pfam02353  43 EEAQQAKLDLILDKlglKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARKRVAAEGLARKvevllqDYRD 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1490190182  96 LPfkeGSFDVVVAVTVLEFVpePKEVLDE----MWRCVRPGGRM---AVGALHEGS 144
Cdd:pfam02353 123 FD---EPFDRIVSVGMFEHV--GHENYDTffkkLYNLLPPGGLMllhTITGLHPDE 173
PRK06202 PRK06202
hypothetical protein; Provisional
 29-199 1.38e-04

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 41.52  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  29 RRAFLRLLEPRVGE----RVLEVGCGTG-------HWTKwfREGLGMRVVGLDLSEGMLAVARARlPEVPLVR-GDATSL 96
Cdd:PRK06202   45 RGLYRRLLRPALSAdrplTLLDIGCGGGdlaidlaRWAR--RDGLRLEVTAIDPDPRAVAFARAN-PRRPGVTfRQAVSD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  97 PFKEGS--FDVVVAVTVLEFV--PEPKEVLDEMWRCVRPG--------GRMAVGALHEGS-PFARRR--RTSGTvLSHAR 161
Cdd:PRK06202  122 ELVAEGerFDVVTSNHFLHHLddAEVVRLLADSAALARRLvlhndlirSRLAYALFWAGTrLLSRSSfvHTDGL-LSVRR 200

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1490190182 162 LFGYDELKELLghygpvrigecvrfpPTGWGVRTSWMF 199
Cdd:PRK06202  201 SYTPAELAALA---------------PQGWRVERQWPF 223
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
33-134 5.19e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 40.14  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  33 LRLLE--PRVGERVLEVGCGTGHwtkwfregLGM--------RVVGLDLSEgmLAV--AR--ARLPEVPLvrgdATSLPF 98
Cdd:PRK00517  110 LEALEklVLPGKTVLDVGCGSGI--------LAIaaaklgakKVLAVDIDP--QAVeaARenAELNGVEL----NVYLPQ 175

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490190182  99 KEGSFDVVVA---VTVLefvpepKEVLDEMWRCVRPGGR 134
Cdd:PRK00517  176 GDLKADVIVAnilANPL------LELAPDLARLLKPGGR 208
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
40-151 8.19e-04

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 40.24  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  40 VGERVLEVGCGTGHWTKWFREGL-GMRVVGLDLSEGMLAV--ARARLPEVP--LVRGDATSLP--FKEGSFDVVVAVTVL 112
Cdd:PRK06922  418 KGDTIVDVGAGGGVMLDMIEEETeDKRIYGIDISENVIDTlkKKKQNEGRSwnVIKGDAINLSssFEKESVDTIVYSSIL 497

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1490190182 113 E----FVPEP---------KEVLDEMWRCVRPGGRMAV--GALHEGSPFARRRR 151
Cdd:PRK06922  498 HelfsYIEYEgkkfnheviKKGLQSAYEVLKPGGRIIIrdGIMTEDKRLMRVIR 551
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 37-133 8.27e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 39.72  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  37 EPRVGERVLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARL---PEVPLVR---GDATSLPFKEGSFDVVVAVT 110
Cdd:PLN02396  128 KPFEGLKFIDIGCGGGLLSEPLAR-MGATVTGVDAVDKNVKIARLHAdmdPVTSTIEylcTTAEKLADEGRKFDAVLSLE 206

                          90       100
                  ....*....|....*....|...
gi 1490190182 111 VLEFVPEPKEVLDEMWRCVRPGG 133
Cdd:PLN02396  207 VIEHVANPAEFCKSLSALTIPNG 229
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
26-175 8.80e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 39.25  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  26 EAERRAFLRLLEPrvGERVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARLPE------VPLVRGDATSLPFK 99
Cdd:COG4076    23 DAFKAAIERVVKP--GDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAAnglsdrITVINADATDLDLP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182 100 EgSFDVVVAVTVLEFVPEPKEV---LDEMWRCVRPGGRM------AVGALHEGSPFARRRRTSGTVLSHARLFGYDELKE 170
Cdd:COG4076   101 E-KADVIISEMLDTALLDEGQVpilNHARKRLLKPGGRIiperitNAAQPVESPVDAEGFEDWQFDGFDFRLFGFLLYAE 179


                  ....*
gi 1490190182 171 LLGHY 175
Cdd:COG4076   180 PLLHL 184
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
33-134 1.18e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 39.00  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  33 LRLLE--PRVGERVLEVGCGTGHwtkwfregLGM--------RVVGLDLSEgmLAV--AR--ARL----PEVPLVRGDAt 94
Cdd:COG2264   139 LEALEklLKPGKTVLDVGCGSGI--------LAIaaaklgakRVLAVDIDP--VAVeaARenAELngveDRIEVVLGDL- 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1490190182  95 slpFKEGSFDVVVA---VTVLefvpepKEVLDEMWRCVRPGGR 134
Cdd:COG2264   208 ---LEDGPYDLVVAnilANPL------IELAPDLAALLKPGGY 241
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 32-134 1.48e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 38.79  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  32 FLRLLEPRVGERVLEVGCGT-GHWTKWFREGLGMR-VVGLDLSEGMLAVARARLPEVPLVRGDATSLPfkEGSFDVVVAV 109
Cdd:cd08255    89 GVRDAEPRLGERVAVVGLGLvGLLAAQLAKAAGAReVVGVDPDAARRELAEALGPADPVAADTADEIG--GRGADVVIEA 166

                          90       100
                  ....*....|....*....|....*
gi 1490190182 110 TvlefvpEPKEVLDEMWRCVRPGGR 134
Cdd:cd08255   167 S------GSPSALETALRLLRDRGR 185
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 23-127 1.74e-03

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 38.78  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  23 AVDEAERRAFLRLLEPRvGERVLEVGCGTGH--W--TKWFREGLgmRVVGLDLSEGMLAVAR--------ARLPEVPLVR 90
Cdd:COG5459    64 AVRAALAELAEAGPDFA-PLTVLDVGAGPGTaaWaaADAWPSLL--DATLLERSAAALALGRrlaraaanPALETAEWRL 140

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1490190182  91 GDATSlPFKEGSFDVVVAVTVLEFVPEPK--EVLDEMWR 127
Cdd:COG5459   141 ADLAA-ALPAPPADLVVASYVLNELADAAraALVDRLWL 178
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 30-172 2.11e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.46  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEPRVGERVLEVGCGT-GHWTKWFREGLGMRVVGLDLSEGMLAVARARLPEVPLVRGD----ATSLPFKEGSFD 104
Cdd:cd05188   124 HALRRAGVLKPGDTVLVLGAGGvGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEedleEELRLTGGGGAD 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490190182 105 VVVavtvlEFVPEPkEVLDEMWRCVRPGGRMA-VGALHEGSPFARRRR--TSGTVLSHARLFGYDELKELL 172
Cdd:cd05188   204 VVI-----DAVGGP-ETLAQALRLLRPGGRIVvVGGTSGGPPLDDLRRllFKELTIIGSTGGTREDFEEAL 268
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 43-133 2.12e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTGHWTKWFREGLGMRVVGLDLSEGMLAVARARLPEVPLVRGDATSL---PFKEGSFDVVVAVTVLEFVP--E 117
Cdd:PTZ00098   55 KVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDIlkkDFPENTFDMIYSRDAILHLSyaD 134

                          90
                  ....*....|....*.
gi 1490190182 118 PKEVLDEMWRCVRPGG 133
Cdd:PTZ00098  135 KKKLFEKCYKWLKPNG 150
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 30-135 2.30e-03

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: 37.57  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  30 RAFLRLLEPRVGERVLEVGCGTGHWTKWF-REGLGMRVVGLDLSEGMLAVARA-----RLPEVPLVRGDATSlPFKEGSF 103
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALaKESPDAELTMVDINARALESAREnlaanGLENGEVVASDVYS-GVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1490190182 104 DVVV---------AVT---VLEFVPEPKEVLdemwrcvRPGGRM 135
Cdd:pfam05175 100 DLIIsnppfhaglATTynvAQRFIADAKRHL-------RPGGEL 136
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 44-108 4.06e-03

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 37.68  E-value: 4.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490190182  44 VLEVGCGTGHWTKWFREgLGMRVVGLDLSEGMLAVARARLPEVPL------VRGDA--TSLPFkegsFDVVVA 108
Cdd:PTZ00338   40 VLEIGPGTGNLTEKLLQ-LAKKVIAIEIDPRMVAELKKRFQNSPLasklevIEGDAlkTEFPY----FDVCVA 107
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 24-133 4.54e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.81  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  24 VDEAERRAFLRLLEPRVGERVLEVGCGTGHWTKWFREGLGmRVVGLDLSEGML---AVARARLPEVPLVRGDATS--LPF 98
Cdd:PLN02336   21 LDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAG-QVIALDFIESVIkknESINGHYKNVKFMCADVTSpdLNI 99

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490190182  99 KEGSFDVVVAVTVLEFVP--EPKEVLDEMWRCVRPGG 133
Cdd:PLN02336  100 SDGSVDLIFSNWLLMYLSdkEVENLAERMVKWLKVGG 136
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 24-108 4.74e-03

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 37.41  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  24 VDEAERRAFLRLLEPRVGERVLEVGCGTGHWTkwfrEGL---GMRVVGLDLSEGMLAVARARLPEVP---LVRGDATSLP 97
Cdd:COG0030    21 IDPNIIRRIVDAAGITPGDTVLEIGPGLGALT----RALlerAARVTAVEIDRRLAAILRETFAAYPnltVIEGDALKVD 96

                          90
                  ....*....|....
gi 1490190182  98 FKE---GSFDVVVA 108
Cdd:COG0030    97 LPAlaaGEPLKVVG 110
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 43-135 4.83e-03

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 37.41  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490190182  43 RVLEVGCGTG-HWTKWFREGLGmRVVGLDLSEGMLAVARARLP-------------EVPLVRGDATS------LPFKEGS 102
Cdd:pfam03291  66 KVLDLGCGKGgDLEKWFKGGIS-QLIGTDIAEVSIEQCRERYNklrsgnkskyykfDAEFITGDCFVsslrevFEDPFGK 144

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1490190182 103 FDVVVAVTVLEFVPEPKEVLDEMWR----CVRPGGRM 135
Cdd:pfam03291 145 FDIVSCQFAIHYSFESEEKARTMLRnvaeLLASGGVF 181
 
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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