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Conserved domains on  [gi|1935375888|gb|QPG05978|]
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bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE [Salinimonas marina]

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
SCOP:  3000118

Graphical summary

 Zoom to residue level

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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 ...
26-264 2.68e-149

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


:

Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 416.48  E-value: 2.68e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  26 FKQVEKSQKASMVANVFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVT 105
Cdd:PRK00216    1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 106 LADINLSMLKVGRDKLRDKGLVSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFS 185
Cdd:PRK00216   81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935375888 186 KPASEHLSKLYDVYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVALHRGYKF 264
Cdd:PRK00216  161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
26-264 2.68e-149

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 416.48  E-value: 2.68e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  26 FKQVEKSQKASMVANVFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVT 105
Cdd:PRK00216    1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 106 LADINLSMLKVGRDKLRDKGLVSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFS 185
Cdd:PRK00216   81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935375888 186 KPASEHLSKLYDVYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVALHRGYKF 264
Cdd:PRK00216  161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
38-263 1.03e-118

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 338.64  E-value: 1.03e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  38 VANVFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVG 117
Cdd:pfam01209   4 VGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 118 RDKLRDKGlVSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKLYD 197
Cdd:pfam01209  84 EKKAKEEG-KYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYE 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935375888 198 VYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVALHRGYK 263
Cdd:pfam01209 163 LYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
38-263 1.08e-116

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: 333.46  E-value: 1.08e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  38 VANVFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVG 117
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 118 RDKLRDKglvSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKLYD 197
Cdd:TIGR01934  81 KKKSELP---LNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935375888 198 VYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVALHRGYK 263
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
42-195 3.17e-44

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: 146.29  E-value: 3.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  42 FDSVAAKYDVmndlmslgvhrlwKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMvgpTGSVTLADINLSMLKVGRDKL 121
Cdd:COG2226     1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935375888 122 RDKGLvsNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKL 195
Cdd:COG2226    65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
79-181 9.96e-15

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: 68.23  E-value: 9.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  79 KVLDIAGGTGDLTAKFSRmvGPTGSVTLADINLSMLKVGRdKLRDKGLVSNIDYVQADAESLPF-PDNTFDVVTMAFGLR 157
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLH 77
                          90       100
                  ....*....|....*....|....*
gi 1935375888 158 -NVTEKQNALNSIYRVLKPGGRLLV 181
Cdd:cd02440    78 hLVEDLARFLEEARRLLKPGGVLVL 102
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
79-184 1.05e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888   79 KVLDIAGGTG----DLTAKFS--RMVGPTGSVTLAdinlsmlKVGRDKLRDKGLVSNIDYVQADAESLPFPDnTFDVVtm 152
Cdd:smart00828   2 RVLDFGCGYGsdliDLAERHPhlQLHGYTISPEQA-------EVGRERIRALGLQGRIRIFYRDSAKDPFPD-TYDLV-- 71
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1935375888  153 aFGLRNVT---EKQNALNSIYRVLKPGGRLLVLEF 184
Cdd:smart00828  72 -FGFEVIHhikDKMDLFSNISRHLKDGGHLVLADF 105
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
26-264 2.68e-149

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 416.48  E-value: 2.68e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  26 FKQVEKSQKASMVANVFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVT 105
Cdd:PRK00216    1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 106 LADINLSMLKVGRDKLRDKGLVSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFS 185
Cdd:PRK00216   81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935375888 186 KPASEHLSKLYDVYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVALHRGYKF 264
Cdd:PRK00216  161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
38-263 1.03e-118

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 338.64  E-value: 1.03e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  38 VANVFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVG 117
Cdd:pfam01209   4 VGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 118 RDKLRDKGlVSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKLYD 197
Cdd:pfam01209  84 EKKAKEEG-KYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYE 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935375888 198 VYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVALHRGYK 263
Cdd:pfam01209 163 LYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
38-263 1.08e-116

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: 333.46  E-value: 1.08e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  38 VANVFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVG 117
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 118 RDKLRDKglvSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKLYD 197
Cdd:TIGR01934  81 KKKSELP---LNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935375888 198 VYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVALHRGYK 263
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
41-256 4.65e-45

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 152.35  E-value: 4.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  41 VFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVG--R 118
Cdd:PLN02233   38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 119 DKLRDKGLVSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKLYDV 198
Cdd:PLN02233  118 QELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEW 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1935375888 199 YSFHILPRMGQVVANDEEsYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIV 256
Cdd:PLN02233  198 MIDNVVVPVATGYGLAKE-YEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLM 254
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
42-195 3.17e-44

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: 146.29  E-value: 3.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  42 FDSVAAKYDVmndlmslgvhrlwKRYTIDCSGVRAGHKVLDIAGGTGDLTAKFSRMvgpTGSVTLADINLSMLKVGRDKL 121
Cdd:COG2226     1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1935375888 122 RDKGLvsNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKL 195
Cdd:COG2226    65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
80-177 4.23e-30

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 108.42  E-value: 4.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  80 VLDIAGGTGDLTAKFSRMVGptGSVTLADINLSMLKVGRDKLRDKGLvsNIDYVQADAESLPFPDNTFDVVTMAFGLRNV 159
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL 76
                          90       100
                  ....*....|....*....|
gi 1935375888 160 TEKQ--NALNSIYRVLKPGG 177
Cdd:pfam13649  77 PDPDleAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
74-252 1.30e-25

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 100.78  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVGRDklRDKGLVSNIDYVQADAESLPFPDNTFDVVTMA 153
Cdd:PRK08317   17 VQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDADGLPFPDGSFDAVRSD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 154 FGLRNVTEKQNALNSIYRVLKPGGRLLVLE-------FSKPASEHLSKLYDVYSFHIL-PRMGqvvandeesyRYLAesi 225
Cdd:PRK08317   95 RVLQHLEDPARALAEIARVLRPGGRVVVLDtdwdtlvWHSGDRALMRKILNFWSDHFAdPWLG----------RRLP--- 161
                         170       180
                  ....*....|....*....|....*....
gi 1935375888 226 rmhpdqetlkGMFEQAGF--EQCDYSNLT 252
Cdd:PRK08317  162 ----------GLFREAGLtdIEVEPYTLI 180
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
81-181 1.12e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 91.57  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  81 LDIAGGTGDLTAKFSRMVGptgSVTLADINLSMLKVGRDKLRDKGLvsniDYVQADAESLPFPDNTFDVVTMAFGLRNVT 160
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPFPDNSFDLVLSSEVLHHVE 73
                          90       100
                  ....*....|....*....|.
gi 1935375888 161 EKQNALNSIYRVLKPGGRLLV 181
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
74-181 3.87e-22

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: 88.54  E-value: 3.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLDIAGGTGDLTAKFSRMvgptG-SVTLADINLSMLKVGRDKLRDkglvSNIDYVQADAESLPFPDNTFDVVTM 152
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARR----GaDVTGVDISPEALEIARERAAE----LNVDFVQGDLEDLPLEDGSFDLVIC 93
                          90       100
                  ....*....|....*....|....*....
gi 1935375888 153 AFGLRNVTEKQNALNSIYRVLKPGGRLLV 181
Cdd:COG2227    94 SEVLEHLPDPAALLRELARLLKPGGLLLL 122
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
118-257 1.22e-18

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 80.50  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 118 RDKLRDKGLVSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKpASEHLSKLYD 197
Cdd:PLN02232   16 RQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFNK-SNQSVTTFMQ 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 198 VYSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQAGFEQCDYSNLTGGIVA 257
Cdd:PLN02232   95 GWMIDNVVVPVATVYDLAKEYEYLKYSINGYLTGEELETLALEAGFSSACHYEISGGFMG 154
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
42-205 4.01e-18

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: 80.79  E-value: 4.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  42 FDSVAAKYDVMNDLMSLGVHRLWKRytIDCSGVRAGHKVLDIAGGTGDLTAKFSRMvGPTGSVTLADINLSMLKVGRDKL 121
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLAL--LKEKGIFIPASVLDIGCGTGYLTRALLKR-FPQAEFIALDISAGMLAQAKTKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 122 RdkglvSNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGrllVLEFSKPASEHLSKLYDVYSF 201
Cdd:TIGR02072  79 S-----ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGG---LLAFSTFGPGTLHELRQSFGQ 150

                  ....
gi 1935375888 202 HILP 205
Cdd:TIGR02072 151 HGLR 154
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
75-242 5.45e-18

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 78.23  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  75 RAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVGRDKLRDKGLvSNIDYVQADAESLP--FPDNTFDVVTM 152
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPelLEDDKFDVVIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 153 AFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSkpasehlsklydvysfhilpRMGQVVANDEESYRYLAESIRMHPDQE 232
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD--------------------SLAELPAHVKEDSTYYAGCVGGAILKK 140
                         170
                  ....*....|
gi 1935375888 233 TLKGMFEQAG 242
Cdd:pfam13847 141 KLYELLEEAG 150
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
76-181 5.33e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 74.09  E-value: 5.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  76 AGHKVLDIAGGTGDLTAKFSRMVgPTGSVTLADINLSMLKVGRDKLrdkglvSNIDYVQADAESLPfPDNTFDVVTMAFG 155
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLD-PPEPFDLVVSNAA 72
                          90       100
                  ....*....|....*....|....*.
gi 1935375888 156 LRNVTEKQNALNSIYRVLKPGGRLLV 181
Cdd:COG4106    73 LHWLPDHAALLARLAAALAPGGVLAV 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
38-180 2.68e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 71.95  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  38 VANVFDSVAAKYDvmNDLMSLGVHRLWKRY---TIDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGptgSVTLADINLSML 114
Cdd:COG4976     7 VEALFDQYADSYD--AALVEDLGYEAPALLaeeLLARLPPGPFGRVLDLGCGTGLLGEALRPRGY---RLTGVDLSEEML 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1935375888 115 kvgrDKLRDKGLvsNIDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRLL 180
Cdd:COG4976    82 ----AKAREKGV--YDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
81-179 6.13e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 68.55  E-value: 6.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  81 LDIAGGTGDLTAKFSRMVgPTGSVTLADINLSMLKVGRDKLRDKGL--VSNIDYVQADAESLPFPdnTFDVVTMAFGLRN 158
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAL-PGLEYTGLDISPAALEAARERLAALGLlnAVRVELFQLDLGELDPG--SFDVVVASNVLHH 77
                          90       100
                  ....*....|....*....|.
gi 1935375888 159 VTEKQNALNSIYRVLKPGGRL 179
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
79-181 9.96e-15

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: 68.23  E-value: 9.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  79 KVLDIAGGTGDLTAKFSRmvGPTGSVTLADINLSMLKVGRdKLRDKGLVSNIDYVQADAESLPF-PDNTFDVVTMAFGLR 157
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLH 77
                          90       100
                  ....*....|....*....|....*
gi 1935375888 158 -NVTEKQNALNSIYRVLKPGGRLLV 181
Cdd:cd02440    78 hLVEDLARFLEEARRLLKPGGVLVL 102
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
73-181 4.32e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 68.03  E-value: 4.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  73 GVRAGHKVLDIAGGTGDLTAKFSRMVGptGSVTLADINLSMLKVGRDKLRDKGLVSNIDYVQADAESLPfPDNTFDVV-- 150
Cdd:COG2230    48 GLKPGMRVLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFDAIvs 124
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1935375888 151 ---TMAFGLRNVTEkqnALNSIYRVLKPGGRLLV 181
Cdd:COG2230   125 igmFEHVGPENYPA---YFAKVARLLKPGGRLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
79-181 6.12e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 68.40  E-value: 6.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  79 KVLDIAGGTGDLTAKFSRMVGptGSVTLADINLSMLKVGRDKLRDKGLvSNIDYVQAD-AESLPFPDNTFDVVTmAFGLR 157
Cdd:COG0500    29 RVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADlAELDPLPAESFDLVV-AFGVL 104
                          90       100
                  ....*....|....*....|....*..
gi 1935375888 158 NVTEKQN---ALNSIYRVLKPGGRLLV 181
Cdd:COG0500   105 HHLPPEEreaLLRELARALKPGGVLLL 131
arsM PRK11873
arsenite methyltransferase;
75-245 1.81e-13

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 68.44  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  75 RAGHKVLDIAGGTG-D--LTAkfsRMVGPTGSVTLADINLSMLKVGRDKLRdKGLVSNIDYVQADAESLPFPDNTFDVVt 151
Cdd:PRK11873   76 KPGETVLDLGSGGGfDcfLAA---RRVGPTGKVIGVDMTPEMLAKARANAR-KAGYTNVEFRLGEIEALPVADNSVDVI- 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 152 mafgLRN-----VTEKQNALNSIYRVLKPGGRLLVlefskpaSEhlsklydvysfhilprmgqVVANDEesyryLAESIR 226
Cdd:PRK11873  151 ----ISNcvinlSPDKERVFKEAFRVLKPGGRFAI-------SD-------------------VVLRGE-----LPEEIR 195
                         170       180       190
                  ....*....|....*....|....*....|
gi 1935375888 227 MHPD-----------QETLKGMFEQAGFEQ 245
Cdd:PRK11873  196 NDAElyagcvagalqEEEYLAMLAEAGFVD 225
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
72-197 2.53e-13

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: 67.49  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  72 SGVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVGRDKLRDKGLVSNIDYVQADAESlPFPDNTFDVVT 151
Cdd:COG2519    87 LDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIRE-GIDEGDVDAVF 165
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1935375888 152 MafglrNVTEKQNALNSIYRVLKPGGRLLVLefsKPASEHLSKLYD 197
Cdd:COG2519   166 L-----DMPDPWEALEAVAKALKPGGVLVAY---VPTVNQVSKLVE 203
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
73-244 1.87e-11

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 62.63  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  73 GVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLA-----DINLSMLKVGRDKLR-----DKGLVSNIDYVQADAESLPF 142
Cdd:COG4798    63 GVKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAAnfdpdSEPPEYAKRSREAFSaklaaDPALYGNVRVTAFAPPDDPI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 143 -PDNTFDVVTMAfglRNV------TEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSklydvysfhilprmgqvvanDE 215
Cdd:COG4798   143 aPPGSADLVLTF---RNYhnwyraGDAAAMFAAFFKALKPGGVLGVVDHRAPPGTGLE--------------------AV 199
                         170       180
                  ....*....|....*....|....*....
gi 1935375888 216 ESYRYLaesirmhpDQETLKGMFEQAGFE 244
Cdd:COG4798   200 ATLGYI--------DEAYVIALAEAAGFE 220
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
38-179 1.56e-09

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 56.69  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  38 VANVFDSVAAKYDVMNDLMSLGVHRLwkrytIDCSGVRAGHKVLDIAGGTGDLtakfSRMVGPTGS-VTLADINLSMLKV 116
Cdd:PRK10258    9 IAAAFGRAAAHYEQHAELQRQSADAL-----LAMLPQRKFTHVLDAGCGPGWM----SRYWRERGSqVTALDLSPPMLAQ 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1935375888 117 GRDKLRDKglvsniDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKPGGRL 179
Cdd:PRK10258   80 ARQKDAAD------HYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVV 136
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
75-244 2.35e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 55.13  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  75 RAGHKVLDIAGGTGDLTAKFSRmVGPTgsVTLADINLSMlkvgrdklrDKGLVSNIDYVQADAESLPFPDNTFDVVTMAF 154
Cdd:pfam13489  21 PSPGRVLDFGCGTGIFLRLLRA-QGFS--VTGVDPSPIA---------IERALLNVRFDQFDEQEAAVPAGKFDVIVARE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 155 GLRNVTEKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKLYDVYSFHILPRMgqvvandeeSYrylaesirmhPDQETL 234
Cdd:pfam13489  89 VLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHI---------SL----------FSARSL 149
                         170
                  ....*....|
gi 1935375888 235 KGMFEQAGFE 244
Cdd:pfam13489 150 KRLLEEAGFE 159
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
66-211 2.74e-09

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: 54.95  E-value: 2.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  66 RYTIDCSGVRAGHKVLDIAGGTGdLTAKFSRMVGPTgsVTLADINLSMLKVGRDKLRDKGLvSNIDYVQADAESLPFPDN 145
Cdd:COG1041    16 RALVNLAGAKEGDTVLDPFCGTG-TILIEAGLLGRR--VIGSDIDPKMVEGARENLEHYGY-EDADVIRGDARDLPLADE 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1935375888 146 TFD-VVT-MAFGLRNVTEK-------QNALNSIYRVLKPGGRlLVLEFSKPASEHLSKLYdvysFHILPRMGQVV 211
Cdd:COG1041    92 SVDaIVTdPPYGRSSKISGeellelyEKALEEAARVLKPGGR-VVIVTPRDIDELLEEAG----FKVLERHEQRV 161
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
79-178 2.49e-08

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 53.74  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  79 KVLDIAGGTGDLTAKFSRMVGPtGSVTLADINLSMLKvgrdKLRDKGLVSNIDYVQADAESLPFPDNTFDVVTMAFGLRN 158
Cdd:PLN02490  116 KVVDVGGGTGFTTLGIVKHVDA-KNVTILDQSPHQLA----KAKQKEPLKECKIIEGDAEDLPFPTDYADRYVSAGSIEY 190
                          90       100
                  ....*....|....*....|
gi 1935375888 159 VTEKQNALNSIYRVLKPGGR 178
Cdd:PLN02490  191 WPDPQRGIKEAYRVLKIGGK 210
PRK05785 PRK05785
hypothetical protein; Provisional
41-240 2.96e-08

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 52.77  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  41 VFDSVAAKYDVMNDLMSLGVHRLWKRYTIDCSGVRAGH--KVLDIAGGTGDLTAKFSRMVgpTGSVTLADINLSMLKVGr 118
Cdd:PRK05785   14 AYNKIPKAYDRANRFISFNQDVRWRAELVKTILKYCGRpkKVLDVAAGKGELSYHFKKVF--KYYVVALDYAENMLKMN- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 119 dklrdkgLVSNiDYVQADAESLPFPDNTFDVVTMAFGLRNVTEKQNALNSIYRVLKpgGRLLVLEFSKPASEHLSKLYDV 198
Cdd:PRK05785   91 -------LVAD-DKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR--KQVGFIAMGKPDNVIKRKYLSF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1935375888 199 YSFHILPRMGQVVANDEESYRYLAESIRMHPDQETLKGMFEQ 240
Cdd:PRK05785  161 YLRYIMPYIACLAGAKCRDYKYIYYIYERLPTNSFHREIFEK 202
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
74-180 9.34e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.49  E-value: 9.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLDIAGGTGdLTAKFSRMVGPtGSVTLADINLSMLKVGRDKLRDKGLVSNIDYVQADAESLPFPdNTFDVV--- 150
Cdd:COG4076    33 VKPGDVVLDIGTGSG-LLSMLAARAGA-KKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLP-EKADVIise 109
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1935375888 151 TMAFGLrnVTEKQ--NALNSIYRVLKPGGRLL 180
Cdd:COG4076   110 MLDTAL--LDEGQvpILNHARKRLLKPGGRII 139
PLN02244 PLN02244
tocopherol O-methyltransferase
79-181 1.21e-06

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 48.97  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  79 KVLDIAGGTGD----LTAKFSRMVgpTGsvtladINLSMLKVGR--DKLRDKGLVSNIDYVQADAESLPFPDNTFDVV-T 151
Cdd:PLN02244  121 RIVDVGCGIGGssryLARKYGANV--KG------ITLSPVQAARanALAAAQGLSDKVSFQVADALNQPFEDGQFDLVwS 192
                          90       100       110
                  ....*....|....*....|....*....|
gi 1935375888 152 MAFGlRNVTEKQNALNSIYRVLKPGGRLLV 181
Cdd:PLN02244  193 MESG-EHMPDKRKFVQELARVAAPGGRIII 221
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
67-152 2.20e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.21  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  67 YTIDCSGVRAGHKVLDIAGGTGDLtAKFSRMVGPTgSVTLADINLSMLKVGRDKLRDKGlvSNIDYVQADAESLPfPDNT 146
Cdd:COG2263    36 HLAYLRGDIEGKTVLDLGCGTGML-AIGAALLGAK-KVVGVDIDPEALEIARENAERLG--VRVDFIRADVTRIP-LGGS 110

                  ....*.
gi 1935375888 147 FDVVTM 152
Cdd:COG2263   111 VDTVVM 116
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
73-181 4.34e-06

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 46.21  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  73 GVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVGRDKLRDKGLvSNIDYVQADAeSLPFPDNT-FDVVT 151
Cdd:pfam01135  70 ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGL-ENVIVVVGDG-RQGWPEFApYDAIH 147
                          90       100       110
                  ....*....|....*....|....*....|
gi 1935375888 152 MAFGLRNVTEkqnalnSIYRVLKPGGRLLV 181
Cdd:pfam01135 148 VGAAAPEIPE------ALIDQLKEGGRLVI 171
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
74-190 6.10e-06

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 47.05  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLD----IAGGTGDLTAKFS-RMVGptgsvtlADINLSMLKVGRDklRDKGLVSNIDYVQADAESLPFPDNTFD 148
Cdd:PLN02336  264 LKPGQKVLDvgcgIGGGDFYMAENFDvHVVG-------IDLSVNMISFALE--RAIGRKCSVEFEVADCTKKTYPDNSFD 334
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1935375888 149 VVTMAFGLRNVTEKQNALNSIYRVLKPGGRLLVLEFSK----PASE 190
Cdd:PLN02336  335 VIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRspgtPSPE 380
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
77-181 6.20e-06

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 46.76  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  77 GHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVGRDKLRDKGlVSNIDYVQADAESLPFPDNTFDVVTMAFGL 156
Cdd:PRK13943   81 GMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLG-IENVIFVCGDGYYGVPEFAPYDVIFVTVGV 159
                          90       100
                  ....*....|....*....|....*
gi 1935375888 157 RNVTEkqnalnSIYRVLKPGGRLLV 181
Cdd:PRK13943  160 DEVPE------TWFTQLKEGGRVIV 178
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
74-181 6.28e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 45.85  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLDIAGGTGDLTAKFSRMVgptGSVTLADINLSMLKVGRDKLRDKGLvSNIDYVQADAeSLPFPDN-TFDVVTM 152
Cdd:COG2518    64 LKPGDRVLEIGTGSGYQAAVLARLA---GRVYSVERDPELAERARERLAALGY-DNVTVRVGDG-ALGWPEHaPFDRIIV 138
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1935375888 153 AFGLRNVTE---KQnalnsiyrvLKPGGRLLV 181
Cdd:COG2518   139 TAAAPEVPEallEQ---------LAPGGRLVA 161
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
76-181 1.06e-05

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: 45.36  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  76 AGHKVLDIAGGTGDLTAKFSRMvgpTGSVTLADINLSMLKVGRDKLRDKGLvsNIDYVQADAESLPF-PDNTFDVVTMAF 154
Cdd:TIGR01983  46 DGLRVLDVGCGGGLLSEPLARL---GANVTGIDASEENIEVAKLHAKKDPL--QIDYRCTTVEDLAEkKAGSFDVVTCME 120
                          90       100
                  ....*....|....*....|....*..
gi 1935375888 155 GLRNVTEKQNALNSIYRVLKPGGRLLV 181
Cdd:TIGR01983 121 VLEHVPDPQAFIRACAQLLKPGGILFF 147
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
80-179 4.59e-05

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 43.80  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  80 VLDIAGGTGDLTAKFSRMvgptG-SVTLADINLSMLKVGRDKLRDKGLVSNIDYVQADAESL-PFPDNTFDVVTMAFGLR 157
Cdd:PRK11036   48 VLDAGGGEGQTAIKLAEL----GhQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIaQHLETPVDLILFHAVLE 123
                          90       100
                  ....*....|....*....|..
gi 1935375888 158 NVTEKQNALNSIYRVLKPGGRL 179
Cdd:PRK11036  124 WVADPKSVLQTLWSVLRPGGAL 145
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
128-228 8.32e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 41.78  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 128 SNIDYVQADAESLPFPDNTFDVVTMA-----FGLRNVtekQNALNSIYRVLKPGGRLLV----LEFSKPASEHLSKLYDV 198
Cdd:COG4627    28 PGVDIVGDLTDPLPFPDNSVDAIYSShvlehLDYEEA---PLALKECYRVLKPGGILRIvvpdLEHVARLYLAEYDAALD 104
                          90       100       110
                  ....*....|....*....|....*....|
gi 1935375888 199 YSFHIlpRMGQVVANDEESYRYLAESIRMH 228
Cdd:COG4627   105 VAELR--LAGPIDPLGIILGERLAGLAARH 132
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
74-181 2.25e-04

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: 40.65  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLDIAGGTGDLTAKFSRMvGPTGSVTLADINLSMLKVGRDKLRDKGLvSNIDYVQADAESlPFPDNTFDVVTM- 152
Cdd:pfam05175  29 KDLSGKVLDLGCGAGVLGAALAKE-SPDAELTMVDINARALESARENLAANGL-ENGEVVASDVYS-GVEDGKFDLIISn 105
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1935375888 153 ----AFGLRNVTEKQNALNSIYRVLKPGGRLLV 181
Cdd:pfam05175 106 ppfhAGLATTYNVAQRFIADAKRHLRPGGELWI 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
79-181 6.46e-04

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: 39.79  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  79 KVLDIAGGTGDLTAKFSRMvGPTGSVTLADINLSMLKVGRDKLRDKGLvSNIDYVQADAESlPFPDNTFDVVTM------ 152
Cdd:COG2813    52 RVLDLGCGYGVIGLALAKR-NPEARVTLVDVNARAVELARANAAANGL-ENVEVLWSDGLS-GVPDGSFDLILSnppfha 128
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1935375888 153 -AFGLRNVTEK--QNAlnsiYRVLKPGGRLLV 181
Cdd:COG2813   129 gRAVDKEVAHAliADA----ARHLRPGGELWL 156
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
79-184 1.05e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888   79 KVLDIAGGTG----DLTAKFS--RMVGPTGSVTLAdinlsmlKVGRDKLRDKGLVSNIDYVQADAESLPFPDnTFDVVtm 152
Cdd:smart00828   2 RVLDFGCGYGsdliDLAERHPhlQLHGYTISPEQA-------EVGRERIRALGLQGRIRIFYRDSAKDPFPD-TYDLV-- 71
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1935375888  153 aFGLRNVT---EKQNALNSIYRVLKPGGRLLVLEF 184
Cdd:smart00828  72 -FGFEVIHhikDKMDLFSNISRHLKDGGHLVLADF 105
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
76-199 2.44e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  76 AGHKVLDIAGGTGDLTAKFSRMVGptGSVTLADINLSMLKVGRDKLRDKglvSNIDYVQADAESLPFPDNTFDVVTMAFG 155
Cdd:PTZ00098   52 ENSKVLDIGSGLGGGCKYINEKYG--AHVHGVDICEKMVNIAKLRNSDK---NKIEFEANDILKKDFPENTFDMIYSRDA 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1935375888 156 LRNVT--EKQNALNSIYRVLKPGGRLLVLEFSKPASEHLSKLYDVY 199
Cdd:PTZ00098  127 ILHLSyaDKKKLFEKCYKWLKPNGILLITDYCADKIENWDEEFKAY 172
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
74-195 2.53e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 37.85  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVGRDKLRDKGLVSNIDYVQADA-ESLPFPDNTFDVVTM 152
Cdd:PRK00377   38 LRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEApEILFTINEKFDRIFI 117
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1935375888 153 AFGLRNVTEkqnALNSIYRVLKPGGRLLV----LEFSKPASEHLSKL 195
Cdd:PRK00377  118 GGGSEKLKE---IISASWEIIKKGGRIVIdailLETVNNALSALENI 161
rADc smart00650
Ribosomal RNA adenine dimethylases;
69-150 4.60e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888   69 IDCSGVRAGHKVLDIAGGTGDLTAKFSRMVGPtgsVTLADINLSMLKVGRDKLRDKglvSNIDYVQADAESLPFPDNTFD 148
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGALTEELLERAKR---VTAIEIDPRLAPRLREKFAAA---DNLTVIHGDALKFDLPKLQPY 79

                   ..
gi 1935375888  149 VV 150
Cdd:smart00650  80 KV 81
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
74-247 5.04e-03

carboxy-S-adenosyl-L-methionine synthase CmoA;


Pssm-ID: 185348  Cd Length: 247  Bit Score: 37.31  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  74 VRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLA-DINLSMLKVGRDKLRDKGLVSNIDYVQADAESLPFPDNTFDVVTM 152
Cdd:PRK15451   54 VQPGTQVYDLGCSLGAATLSVRRNIHHDNCKIIAiDNSPAMIERCRRHIDAYKAPTPVDVIEGDIRDIAIENASMVVLNF 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888 153 AFGLRNVTEKQNALNSIYRVLKPGGRLLVLE-FSKPASEHLSKLYDVYsfHILPRMGQVVANDEESYRYLAESIRMHPDQ 231
Cdd:PRK15451  134 TLQFLEPSERQALLDKIYQGLNPGGALVLSEkFSFEDAKVGELLFNMH--HDFKRANGYSELEISQKRSMLENVMLTDSV 211
                         170
                  ....*....|....*.
gi 1935375888 232 ETLKGMFEQAGFEQCD 247
Cdd:PRK15451  212 ETHKARLHKAGFEHSE 227
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
61-143 5.06e-03

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 37.47  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  61 HRLWKRYTIDCS------GVRAGHKVLDIAGGTGDLTAKFSRMVGPTGSVTLADINLSMLKVGRDKLRDKGLVSNIDYVQ 134
Cdd:pfam08704  19 HRTQILYTPDISlitmmlELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADKAREEFREHGIDQLVTVTH 98

                  ....*....
gi 1935375888 135 ADAESLPFP 143
Cdd:pfam08704  99 RDVCKEGFL 107
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
72-182 5.71e-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: 37.30  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935375888  72 SGVRAGHKVLDI-AGGTGDLTAKFSRMVGPTgsVTLADINLSMLkvgrDKLRDKGLVSNIDYVQAD--AESLPFPDNTFD 148
Cdd:cd05188   130 GVLKPGDTVLVLgAGGVGLLAAQLAKAAGAR--VIVTDRSDEKL----ELAKELGADHVIDYKEEDleEELRLTGGGGAD 203
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1935375888 149 VVTMAFGlrnvteKQNALNSIYRVLKPGGRLLVL 182
Cdd:cd05188   204 VVIDAVG------GPETLAQALRLLRPGGRIVVV 231
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
76-150 7.29e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 36.74  E-value: 7.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1935375888  76 AGHKVLDiAG-GTGDLTAKFSRMvgptG-SVTLADINLSMLKVGRDKLRDKGLVSNIDYVQADAESLpfpDNTFDVV 150
Cdd:PRK07580   63 TGLRILD-AGcGVGSLSIPLARR----GaKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLESL---LGRFDTV 131
 
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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