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Conserved domains on  [gi|254789965|sp|B4TBR3|]
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RecName: Full=Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE; AltName: Full=2-methoxy-6-polyprenyl-1,4-benzoquinol methylase; AltName: Full=Demethylmenaquinone methyltransferase

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10011316)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0032259|GO:1904047
PubMed:  9045837|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 13-251 5.58e-152

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


:

Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 422.64  E-value: 5.58e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  13 FQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVI 92
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  93 LADINDSMLKMGREKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFS 172
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254789965 173 KPIIEPLSKAYDAYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF 251
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 13-251 5.58e-152

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 422.64  E-value: 5.58e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  13 FQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVI 92
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  93 LADINDSMLKMGREKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFS 172
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254789965 173 KPIIEPLSKAYDAYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF 251
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
25-250 8.40e-137

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 384.10  E-value: 8.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   25 VAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMG 104
Cdd:pfam01209   4 VGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  105 REKLRNIGVIgNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYD 184
Cdd:pfam01209  84 EKKAKEEGKY-NIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254789965  185 AYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYK 250
Cdd:pfam01209 163 LYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 25-250 5.30e-123

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: 348.87  E-value: 5.30e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   25 VAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMG 104
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  105 REKLRnigVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYD 184
Cdd:TIGR01934  81 KKKSE---LPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254789965  185 AYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYK 250
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 29-174 1.56e-41

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: 138.97  E-value: 1.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  29 FHSVASKYDVMNDLmsfgIHRLwkrftidcsGVRRGQTVLDLAGGTGDLTAKFSRMvgeTGKVILADINDSMLKMGREKL 108
Cdd:COG2226    1 FDRVAARYDGREAL----LAAL---------GLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254789965 109 RNIGVigNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKP 174
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPP 128
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-168 3.01e-13

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: 63.99  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  66 TVLDLAGGTGDLTAKFSRMVGetGKVILADINDSMLKMGREKLRNiGVIGNVEYVQANAEALPF-PDNTFD-CITISFGL 143
Cdd:cd02440    1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 254789965 144 RNVTEKEKALRSMFRVLKPGGRLLV 168
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 13-251 5.58e-152

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 422.64  E-value: 5.58e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  13 FQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVI 92
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  93 LADINDSMLKMGREKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFS 172
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254789965 173 KPIIEPLSKAYDAYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF 251
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
25-250 8.40e-137

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 384.10  E-value: 8.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   25 VAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMG 104
Cdd:pfam01209   4 VGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  105 REKLRNIGVIgNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYD 184
Cdd:pfam01209  84 EKKAKEEGKY-NIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254789965  185 AYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYK 250
Cdd:pfam01209 163 LYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 25-250 5.30e-123

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: 348.87  E-value: 5.30e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   25 VAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMG 104
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  105 REKLRnigVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYD 184
Cdd:TIGR01934  81 KKKSE---LPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254789965  185 AYSFHILPRIGSMVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYK 250
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 28-243 3.62e-47

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 157.36  E-value: 3.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  28 VFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMG--R 105
Cdd:PLN02233  38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 106 EKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKP----------- 174
Cdd:PLN02233 118 QELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKStqpfttsmqew 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254789965 175 ----IIEPLSKAYDAysfhilprigsmvandADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVV 243
Cdd:PLN02233 198 midnVVVPVATGYGL----------------AKEYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLM 254
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 29-174 1.56e-41

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: 138.97  E-value: 1.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  29 FHSVASKYDVMNDLmsfgIHRLwkrftidcsGVRRGQTVLDLAGGTGDLTAKFSRMvgeTGKVILADINDSMLKMGREKL 108
Cdd:COG2226    1 FDRVAARYDGREAL----LAAL---------GLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254789965 109 RNIGVigNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKP 174
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPP 128
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 67-164 1.35e-29

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 106.49  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   67 VLDLAGGTGDLTAKFSRMVGetGKVILADINDSMLKMGREKLRNIGVigNVEYVQANAEALPFPDNTFDCITISFGLRNV 146
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 254789965  147 T--EKEKALRSMFRVLKPGG 164
Cdd:pfam13649  77 PdpDLEAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 52-171 1.04e-28

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 108.87  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  52 KRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMGREklRNIGVIGNVEYVQANAEALPFPD 131
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDADGLPFPD 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 254789965 132 NTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEF 171
Cdd:PRK08317  86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 68-168 4.85e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 89.65  E-value: 4.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   68 LDLAGGTGDLTAKFSRMVGEtgkVILADINDSMLKMGREKLRNIGVignvEYVQANAEALPFPDNTFDCITISFGLRNVT 147
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR---VTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPFPDNSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 254789965  148 EKEKALRSMFRVLKPGGRLLV 168
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
arsM PRK11873
arsenite methyltransferase;
64-234 8.33e-22

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 91.16  E-value: 8.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  64 GQTVLDLAGGTG-D--LTAkfsRMVGETGKVILADINDSMLKMGREKLRNIGvIGNVEYVQANAEALPFPDNTFDCItIS 140
Cdd:PRK11873  78 GETVLDLGSGGGfDcfLAA---RRVGPTGKVIGVDMTPEMLAKARANARKAG-YTNVEFRLGEIEALPVADNSVDVI-IS 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 141 FGLRN-VTEKEKALRSMFRVLKPGGRL----LVLEfsKPIIEPLSKAYDAYSfhilprigSMVANDADSYRYLaesirmh 215
Cdd:PRK11873 153 NCVINlSPDKERVFKEAFRVLKPGGRFaisdVVLR--GELPEEIRNDAELYA--------GCVAGALQEEEYL------- 215

                        170
                 ....*....|....*....
gi 254789965 216 pdqdtlkAMMQDAGFESVD 234
Cdd:PRK11873 216 -------AMLAEAGFVDIT 227
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 61-168 5.04e-21

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: 85.45  E-value: 5.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  61 VRRGQTVLDLAGGTGDLTAKFSRMVGEtgkVILADINDSMLKMGREKLRNIgvigNVEYVQANAEALPFPDNTFDCITIS 140
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARRGAD---VTGVDISPEALEIARERAAEL----NVDFVQGDLEDLPLEDGSFDLVICS 94

                         90       100
                 ....*....|....*....|....*...
gi 254789965 141 FGLRNVTEKEKALRSMFRVLKPGGRLLV 168
Cdd:COG2227   95 EVLEHLPDPAALLRELARLLKPGGLLLL 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 62-172 5.40e-19

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 80.54  E-value: 5.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   62 RRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMGREKLRNIGVIgNVEYVQANAEALP--FPDNTFDCItI 139
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFD-NVEFEQGDIEELPelLEDDKFDVV-I 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 254789965  140 SFGLRN-VTEKEKALRSMFRVLKPGGRLLVLEFS 172
Cdd:pfam13847  80 SNCVLNhIPDPDKVLQEILRVLKPGGRLIISDPD 113
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 105-244 1.94e-18

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 79.73  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 105 REKLRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKP---------- 174
Cdd:PLN02232  16 RQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFNKSnqsvttfmqg 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254789965 175 -----IIEPLSKAYDAysfhilprigsmvandADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVA 244
Cdd:PLN02232  96 wmidnVVVPVATVYDL----------------AKEYEYLKYSINGYLTGEELETLALEAGFSSACHYEISGGFMG 154
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 29-215 1.11e-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: 79.25  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   29 FHSVASKYDVMNDLMSFGIHRLWKRftIDCSGVRRGQTVLDLAGGTGDLTAKFSRMvGETGKVILADINDSMLKMGREKL 108
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLAL--LKEKGIFIPASVLDIGCGTGYLTRALLKR-FPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  109 RnigviGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSF 188
Cdd:TIGR02072  79 S-----ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGL 153

                         170       180
                  ....*....|....*....|....*....
gi 254789965  189 HILPR--IGSMVANDADSYRYLAESIRMH 215
Cdd:TIGR02072 154 RYLSLdeLKALLKNSFELLTLEEELITLS 182
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
63-168 3.85e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 74.09  E-value: 3.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  63 RGQTVLDLAGGTGDLTAKFSRMVGEtGKVILADINDSMLKMGREKLrnigviGNVEYVQANAEALPfPDNTFDCITISFG 142
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPG-ARVTGVDLSPEMLARARARL------PNVRFVVADLRDLD-PPEPFDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*.
gi 254789965 143 LRNVTEKEKALRSMFRVLKPGGRLLV 168
Cdd:COG4106   73 LHWLPDHAALLARLAAALAPGGVLAV 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 50-168 2.32e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 74.95  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  50 LWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGetGKVILADINDSMLKMGREKLRNIGvIGNVEYVQAN-AEALP 128
Cdd:COG0500   13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADlAELDP 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 254789965 129 FPDNTFDCItISFGLRNVTEKE---KALRSMFRVLKPGGRLLV 168
Cdd:COG0500   90 LPAESFDLV-VAFGVLHHLPPEereALLRELARALKPGGVLLL 131
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
60-235 1.41e-14

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 71.10  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  60 GVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILA-----DINDSMLKMGREKLR-----NIGVIGNVEYVQANAEALPF 129
Cdd:COG4798   63 GVKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAAnfdpdSEPPEYAKRSREAFSaklaaDPALYGNVRVTAFAPPDDPI 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 130 -PDNTFDCITISfglRNV------TEKEKALRSMFRVLKPGGRLLVLEfskpiieplskaydaysfHILPriGSMVANDA 202
Cdd:COG4798  143 aPPGSADLVLTF---RNYhnwyraGDAAAMFAAFFKALKPGGVLGVVD------------------HRAP--PGTGLEAV 199

                        170       180       190
                 ....*....|....*....|....*....|...
gi 254789965 203 DSYRYLaesirmhpDQDTLKAMMQDAGFESVDY 235
Cdd:COG4798  200 ATLGYI--------DEAYVIALAEAAGFELVGE 224
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-168 3.01e-13

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: 63.99  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  66 TVLDLAGGTGDLTAKFSRMVGetGKVILADINDSMLKMGREKLRNiGVIGNVEYVQANAEALPF-PDNTFD-CITISFGL 143
Cdd:cd02440    1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 254789965 144 RNVTEKEKALRSMFRVLKPGGRLLV 168
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
22-167 1.29e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 64.25  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  22 ADMVAHVFHSVASKYDvmNDLMSFGIHRLWKRF---TIDCSGVRRGQTVLDLAGGTGDLTAKFSRMVGEtgkVILADIND 98
Cdd:COG4976    4 DAYVEALFDQYADSYD--AALVEDLGYEAPALLaeeLLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR---LTGVDLSE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254789965  99 SMLKMGREKLRNIgvignvEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLL 167
Cdd:COG4976   79 EMLAKAREKGVYD------RLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 59-185 2.32e-12

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: 64.80  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  59 SGVRRGQTVLDlAG-GTGDLTAKFSRMVGETGKVILADINDSMLKMGREKLRNIGVIGNVEYVQANAEAlPFPDNTFDCI 137
Cdd:COG2519   87 LDIFPGARVLE-AGtGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIRE-GIDEGDVDAV 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 254789965 138 TIsfglrNVTEKEKALRSMFRVLKPGGRLLVLefsKPIIEPLSKAYDA 185
Cdd:COG2519  165 FL-----DMPDPWEALEAVAKALKPGGVLVAY---VPTVNQVSKLVEA 204
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 60-168 3.10e-12

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 62.64  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  60 GVRRGQTVLDLAGGTGDLTAkfsRMVGETG-KVILADINDSMLKMGREKLRNIGVIGNVEYVQANAEALPfPDNTFDCIt 138
Cdd:COG2230   48 GLKPGMRVLDIGCGWGGLAL---YLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFDAI- 122

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 254789965 139 ISFGlrnVTE------KEKALRSMFRVLKPGGRLLV 168
Cdd:COG2230  123 VSIG---MFEhvgpenYPAYFAKVARLLKPGGRLLL 155
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 68-166 1.58e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 59.30  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   68 LDLAGGTGDLTAKFSRMVGEtGKVILADINDSMLKMGREKLR--NIGVIGNVEYVQANAEALPFPdnTFDCITISFGLRN 145
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPG-LEYTGLDISPAALEAARERLAalGLLNAVRVELFQLDLGELDPG--SFDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 254789965  146 VTEKEKALRSMFRVLKPGGRL 166
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 59-194 1.75e-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: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  59 SGVRRGQTVLDLAGGTGdLTAKFSRMVGetGKVILADINDSMLKMGREKLRNIGvIGNVEYVQANAEALPFPDNTFDCI- 137
Cdd:COG1041   22 AGAKEGDTVLDPFCGTG-TILIEAGLLG--RRVIGSDIDPKMVEGARENLEHYG-YEDADVIRGDARDLPLADESVDAIv 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254789965 138 -------TISFGLRNVTEK-EKALRSMFRVLKPGGRlLVLEFSKPIIEPLSKAYdaysFHILPRI 194
Cdd:COG1041   98 tdppygrSSKISGEELLELyEKALEEAARVLKPGGR-VVIVTPRDIDELLEEAG----FKVLERH 157
PRK05785 PRK05785
hypothetical protein; Provisional
 28-208 1.80e-11

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 62.01  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  28 VFHSVASKYDVMNDLMSFGIHRLWKRFTID-----CSGVRRgqtVLDLAGGTGDLTAKFSRMVGEtgKVILADINDSMLK 102
Cdd:PRK05785  14 AYNKIPKAYDRANRFISFNQDVRWRAELVKtilkyCGRPKK---VLDVAAGKGELSYHFKKVFKY--YVVALDYAENMLK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 103 MGREKlrnigvignVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKpgGRLLVLEFSKPiIEPLSKA 182
Cdd:PRK05785  89 MNLVA---------DDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR--KQVGFIAMGKP-DNVIKRK 156

                        170       180
                 ....*....|....*....|....*..
gi 254789965 183 Y-DAYSFHILPRIGSMVANDADSYRYL 208
Cdd:PRK05785 157 YlSFYLRYIMPYIACLAGAKCRDYKYI 183
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-231 1.33e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 55.51  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   47 IHRLWKRFTIDCSGV-RRGQTVLDLAGGTGDLTAKFSRmvgETGKVILADINDSMLKMgreklrnigVIGNVEYVQANAE 125
Cdd:pfam13489   5 RERLLADLLLRLLPKlPSPGRVLDFGCGTGIFLRLLRA---QGFSVTGVDPSPIAIER---------ALLNVRFDQFDEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  126 ALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSFHILPRIgsmvandadSY 205
Cdd:pfam13489  73 EAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHI---------SL 143

                         170       180
                  ....*....|....*....|....*.
gi 254789965  206 rylaesirmhPDQDTLKAMMQDAGFE 231
Cdd:pfam13489 144 ----------FSARSLKRLLEEAGFE 159
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 60-188 3.70e-08

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 53.31  E-value: 3.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  60 GVRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMGREKLRNIGvIGNVEYVQANAEALPFPDNTFDCITI 139
Cdd:PRK13943  77 GLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLG-IENVIFVCGDGYYGVPEFAPYDVIFV 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 254789965 140 SFGLRNVTEkekalrSMFRVLKPGGRLLVlefskPIIEPLSKAYDAYSF 188
Cdd:PRK13943 156 TVGVDEVPE------TWFTQLKEGGRVIV-----PINLKLSRRQPAFLF 193
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 25-166 5.97e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 52.07  E-value: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  25 VAHVFHSVASKYDVMNDLMSFGIHRLWKRFtidcsGVRRGQTVLDLAGGTGDLtakfSRMVGETGKVILA-DINDSMLKM 103
Cdd:PRK10258   9 IAAAFGRAAAHYEQHAELQRQSADALLAML-----PQRKFTHVLDAGCGPGWM----SRYWRERGSQVTAlDLSPPMLAQ 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254789965 104 GREKLRNigvignVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRL 166
Cdd:PRK10258  80 ARQKDAA------DHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVV 136
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 61-185 6.05e-08

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 51.34  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  61 VRRGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMGREKLRNIGVIGNVEYVQANA-EALPFPDNTFDCITI 139
Cdd:PRK00377  38 LRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEApEILFTINEKFDRIFI 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 254789965 140 SFGLRnvtEKEKALRSMFRVLKPGGRLLVlefSKPIIEPLSKAYDA 185
Cdd:PRK00377 118 GGGSE---KLKEIISASWEIIKKGGRIVI---DAILLETVNNALSA 157
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
64-168 1.74e-07

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.06  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965   64 GQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMGREKLRNIGvIGNVEYVQANAEaLPFPDNT-FDCITISFG 142
Cdd:pfam01135  74 GMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLG-LENVIVVVGDGR-QGWPEFApYDAIHVGAA 151

                          90       100
                  ....*....|....*....|....*.
gi 254789965  143 LRNVTEkekalrSMFRVLKPGGRLLV 168
Cdd:pfam01135 152 APEIPE------ALIDQLKEGGRLVI 171
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
61-191 8.32e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.49  E-value: 8.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  61 VRRGQTVLDLAGGTGDLTAKFSRMvgETGKVILADINDSMLKMGREKLRNIGVIGNVEYVQANAEALPFPdNTFDcITIS 140
Cdd:COG4076   33 VKPGDVVLDIGTGSGLLSMLAARA--GAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLP-EKAD-VIIS 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254789965 141 FGLRNVTEKEKALRSMF----RVLKPGGRLLVLEFSKpIIEPLSKAYDAYSFHIL 191
Cdd:COG4076  109 EMLDTALLDEGQVPILNharkRLLKPGGRIIPERITN-AAQPVESPVDAEGFEDW 162
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 61-168 1.14e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 47.78  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  61 VRRGQTVLDLAGGTGDLTAKFSRMVGEtgkVILADINDSMLKMGREKLRNIGvIGNVEYVQANAeALPFPDN-TFDCITI 139
Cdd:COG2518   64 LKPGDRVLEIGTGSGYQAAVLARLAGR---VYSVERDPELAERARERLAALG-YDNVTVRVGDG-ALGWPEHaPFDRIIV 138

                         90       100
                 ....*....|....*....|....*....
gi 254789965 140 SFGLRNVTEkekALRSMfrvLKPGGRLLV 168
Cdd:COG2518  139 TAAAPEVPE---ALLEQ---LAPGGRLVA 161
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 64-186 1.24e-06

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 48.98  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  64 GQTVLDLAGGTGDltAKFSRMVGETGKVILADINDSMLKMGREklRNIGVIGNVEYVQANAEALPFPDNTFDCITISFGL 143
Cdd:PLN02336 267 GQKVLDVGCGIGG--GDFYMAENFDVHVVGIDLSVNMISFALE--RAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTI 342

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 254789965 144 RNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPlSKAYDAY 186
Cdd:PLN02336 343 LHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTP-SPEFAEY 384
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 64-168 1.63e-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: 44.41  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  64 GQTVLDLAGGTGDLTAKFSRMVGETgKVILADINDSMLKMGREKLRNIGViGNVEYVQANAeALPFPDNTFDCItIS--- 140
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRNPEA-RVTLVDVNARAVELARANAAANGL-ENVEVLWSDG-LSGVPDGSFDLI-LSnpp 125

                         90       100       110
                 ....*....|....*....|....*....|..
gi 254789965 141 FGLRNVTEKEkALRSMF----RVLKPGGRLLV 168
Cdd:COG2813  126 FHAGRAVDKE-VAHALIadaaRHLRPGGELWL 156
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
54-137 2.33e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 43.74  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  54 FTIDCSGVRRGQTVLDLAGGTGDLtAKFSRMVGeTGKVILADINDSMLKMGREKLRNIGVigNVEYVQANAEALPfPDNT 133
Cdd:COG2263   36 HLAYLRGDIEGKTVLDLGCGTGML-AIGAALLG-AKKVVGVDIDPEALEIARENAERLGV--RVDFIRADVTRIP-LGGS 110


                 ....
gi 254789965 134 FDCI 137
Cdd:COG2263  111 VDTV 114
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 63-165 2.81e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 44.50  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  63 RGQTVLDLAGGTGDLTAKFSRMVgETGKVILADINDSMLKMGREKlrniGVIGNVEYVQANAEALPFPDNTFDCITISFG 142
Cdd:PLN02490 113 RNLKVVDVGGGTGFTTLGIVKHV-DAKNVTILDQSPHQLAKAKQK----EPLKECKIIEGDAEDLPFPTDYADRYVSAGS 187

                         90       100
                 ....*....|....*....|...
gi 254789965 143 LRNVTEKEKALRSMFRVLKPGGR 165
Cdd:PLN02490 188 IEYWPDPQRGIKEAYRVLKIGGK 210
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
60-244 3.23e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.13  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  60 GVRRGQTVLDLAGGTGdLTAKFSRMVGeTGKVILADINDSMLKMGR-----EKLRNigviGNVEYVQANA-EALP-FPDN 132
Cdd:COG2521  129 GVRRGDRVLDTCTGLG-YTAIEALKRG-AREVITVEKDPNVLELAElnpwsRELAN----ERIKIILGDAsEVIKtFPDE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 133 TFDCItI----SFGLRNVTEKEKALRSMFRVLKPGGRLlvlefskpiieplskaydaysFHilprigsmvandadsyrYL 208
Cdd:COG2521  203 SFDAI-IhdppRFSLAGELYSLEFYRELYRVLKPGGRL---------------------FH-----------------YT 243

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 254789965 209 AESIRMHPDQDTLKAMM---QDAGFESVDYYNLTAGVVA 244
Cdd:COG2521  244 GNPGKKKRGRDVPRGVAerlRKAGFKRVRRVEEAQGVLA 282
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
66-166 5.01e-05

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 43.41  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  66 TVLDLAGGTGdltaKFSRMVGETG-KVILADINDSMLKMGREKLRNIGVIGNVEYVQANAEAL-PFPDNTFDCITISFGL 143
Cdd:PRK11036  47 RVLDAGGGEG----QTAIKLAELGhQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIaQHLETPVDLILFHAVL 122

                         90       100
                 ....*....|....*....|...
gi 254789965 144 RNVTEKEKALRSMFRVLKPGGRL 166
Cdd:PRK11036 123 EWVADPKSVLQTLWSVLRPGGAL 145
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 59-214 9.27e-05

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: 42.69  E-value: 9.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  59 SGVRRGQTVLDL-AGGTGDLTAKFSRMVGetGKVILADINDSMLkmgrEKLRNIGVIGNVEYVQAN--AEALPFPDNTFD 135
Cdd:cd05188  130 GVLKPGDTVLVLgAGGVGLLAAQLAKAAG--ARVIVTDRSDEKL----ELAKELGADHVIDYKEEDleEELRLTGGGGAD 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254789965 136 CITisfglrNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPlskaydAYSFHILPRIGSMVANDADSYRYLAESIRM 214
Cdd:cd05188  204 VVI------DAVGGPETLAQALRLLRPGGRIVVVGGTSGGPPL------DDLRRLLFKELTIIGSTGGTREDFEEALDL 270
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 54-173 1.46e-04

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. 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 includes various 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: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 42.18  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  54 FTIDCSGVRRGQ-----TVLDL-AGGTGDLTAKFSRMVGetGKVILADINDSML----KMGREKLRNIGVIGNVEYVQAN 123
Cdd:cd08261  145 LAIGAHAVRRAGvtagdTVLVVgAGPIGLGVIQVAKARG--ARVIVVDIDDERLefarELGADDTINVGDEDVAARLREL 222

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 254789965 124 AEAlPFPDNTFDCITISfglrnvtekeKALRSMFRVLKPGGRLLVLEFSK 173
Cdd:cd08261  223 TDG-EGADVVIDATGNP----------ASMEEAVELVAHGGRVVLVGLSK 261
PLN02244 PLN02244
tocopherol O-methyltransferase
 112-194 3.13e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 41.27  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 112 GVIGNVEYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSFHIL 191
Cdd:PLN02244 165 GLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVTWCHRDLEPGETSLKPDEQKLL 244


                 ...
gi 254789965 192 PRI 194
Cdd:PLN02244 245 DKI 247
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 63-178 3.33e-04

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: 41.09  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  63 RGQTVLDLAGGTGDLTAKFSRMVGETGKVILADINDSMLKMGREKLRNIGV--IGNVEYVQANAEAlPFPDNTFDCITIS 140
Cdd:COG5459   80 APLTVLDVGAGPGTAAWAAADAWPSLLDATLLERSAAALALGRRLARAAANpaLETAEWRLADLAA-ALPAPPADLVVAS 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 254789965 141 FGLRNVTE--KEKALRSMFrvLKPGGRLLvlefskpIIEP 178
Cdd:COG5459  159 YVLNELADaaRAALVDRLW--LAPDGALL-------IVEP 189
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
127-224 1.01e-03

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 38.69  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965 127 LPFPDNTFDCITIS-----FGLRNVtekEKALRSMFRVLKPGGRLLV----LEFskpIIEPLSKAYDAYSFH-ILPRIGS 196
Cdd:COG4627   40 LPFPDNSVDAIYSShvlehLDYEEA---PLALKECYRVLKPGGILRIvvpdLEH---VARLYLAEYDAALDVaELRLAGP 113

                         90       100
                 ....*....|....*....|....*...
gi 254789965 197 MVANDADSYRYLAESIRMHPDQDTLKAM 224
Cdd:COG4627  114 IDPLGIILGERLAGLAARHSVLFRTGFT 141
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 60-137 3.69e-03

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 38.23  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254789965  60 GVRRGQTVLDLAGGTGDLTAKFSRMVgetGKVILADINDSMLKMGREKLRNIGvIGNVEYVQANAE-ALP--FPDNTFDC 136
Cdd:COG2265  230 DLTGGERVLDLYCGVGTFALPLARRA---KKVIGVEIVPEAVEDARENARLNG-LKNVEFVAGDLEeVLPelLWGGRPDV 305


                 .
gi 254789965 137 I 137
Cdd:COG2265  306 V 306
 
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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