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Conserved domains on  [gi|15600256|ref|NP_253750|]
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ubiquinone/menaquinone biosynthesis methyltransferase [Pseudomonas aeruginosa PAO1]

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 ...
 18-256 4.85e-152

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


:

Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 423.02  E-value: 4.85e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   18 YQNVPESQKAKKVAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVV 97
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   98 LADINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFS 177
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600256  178 KPSSNLLSKAYDAYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVALHRGIKP 256
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 18-256 4.85e-152

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 423.02  E-value: 4.85e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   18 YQNVPESQKAKKVAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVV 97
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   98 LADINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFS 177
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600256  178 KPSSNLLSKAYDAYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVALHRGIKP 256
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
29-255 2.75e-117

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 334.79  E-value: 2.75e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    29 KVAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKV 108
Cdd:pfam01209   3 RVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   109 GRDKLLDKGVSgNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAY 188
Cdd:pfam01209  83 GEKKAKEEGKY-NIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAY 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600256   189 DAYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVALHRGIK 255
Cdd:pfam01209 162 ELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-255 3.80e-112

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: 321.52  E-value: 3.80e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    30 VAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVG 109
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   110 RDKLLDKGvsgNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAYD 189
Cdd:TIGR01934  81 KKKSELPL---NIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600256   190 AYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVALHRGIK 255
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 34-194 1.89e-42

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: 141.28  E-value: 1.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  34 FHSVAAKYDLMNDLmsggihrlwkrftIELSGVRSGNRVLDIAGGTGDLTRQFSRLvgpTGEVVLADINASMLKVGRDKL 113
Cdd:COG2226   1 FDRVAARYDGREAL-------------LAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256 114 LDKGVsgNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAYDAYSF 193
Cdd:COG2226  65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAGF 142


                .
gi 15600256 194 S 194
Cdd:COG2226 143 E 143
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-173 1.41e-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: 70.54  E-value: 1.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  71 RVLDIAGGTGDLTRQFSRLVGptGEVVLADINASMLKVGRDKLLDKGvSGNVSFVQADAEKLPF-PDNHFD-CVTIAFGL 148
Cdd:cd02440   1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPeADESFDvIISDPPLH 77

                        90       100
                ....*....|....*....|....*
gi 15600256 149 RNVTHKDEAIRSMLRVLKPGGRLLV 173
Cdd:cd02440  78 HLVEDLARFLEEARRLLKPGGVLVL 102
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
71-195 2.21e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 47.41  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256     71 RVLDIAGGTG----DLTRQFS--RLVGPTgevvladINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFPDNHfdcvTI 144
Cdd:smart00828   2 RVLDFGCGYGsdliDLAERHPhlQLHGYT-------ISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTY----DL 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15600256    145 AFGLRNVTH---KDEAIRSMLRVLKPGGRLLVLEF-SKPSSNLLSKAYDAYSFSL 195
Cdd:smart00828  71 VFGFEVIHHikdKMDLFSNISRHLKDGGHLVLADFiANLLSAIEHEETTSYLVTR 125
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 18-256 4.85e-152

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 423.02  E-value: 4.85e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   18 YQNVPESQKAKKVAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVV 97
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   98 LADINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFS 177
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600256  178 KPSSNLLSKAYDAYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVALHRGIKP 256
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
29-255 2.75e-117

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 334.79  E-value: 2.75e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    29 KVAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKV 108
Cdd:pfam01209   3 RVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   109 GRDKLLDKGVSgNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAY 188
Cdd:pfam01209  83 GEKKAKEEGKY-NIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAY 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600256   189 DAYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVALHRGIK 255
Cdd:pfam01209 162 ELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-255 3.80e-112

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: 321.52  E-value: 3.80e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    30 VAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVG 109
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   110 RDKLLDKGvsgNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAYD 189
Cdd:TIGR01934  81 KKKSELPL---NIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600256   190 AYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVALHRGIK 255
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 33-248 3.48e-45

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 152.35  E-value: 3.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   33 VFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVG--R 110
Cdd:PLN02233  38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  111 DKLLDKGVSGNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAYD- 189
Cdd:PLN02233 118 QELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEw 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600256  190 AYSFSLLPLmgKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIV 248
Cdd:PLN02233 198 MIDNVVVPV--ATGYGLAKEYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLM 254
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 34-194 1.89e-42

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: 141.28  E-value: 1.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  34 FHSVAAKYDLMNDLmsggihrlwkrftIELSGVRSGNRVLDIAGGTGDLTRQFSRLvgpTGEVVLADINASMLKVGRDKL 113
Cdd:COG2226   1 FDRVAARYDGREAL-------------LAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256 114 LDKGVsgNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAYDAYSF 193
Cdd:COG2226  65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAGF 142


                .
gi 15600256 194 S 194
Cdd:COG2226 143 E 143
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 72-169 3.93e-30

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 108.03  E-value: 3.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    72 VLDIAGGTGDLTRQFSRLVGptGEVVLADINASMLKVGRDKLLDKGVsgNVSFVQADAEKLPFPDNHFDCVTIAFGLRNV 151
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 15600256   152 THKD--EAIRSMLRVLKPGG 169
Cdd:pfam13649  77 PDPDleAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 57-176 1.74e-29

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 110.80  E-value: 1.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   57 KRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDKLLDKGvsGNVSFVQADAEKLPFPD 136
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADGLPFPD 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15600256  137 NHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEF 176
Cdd:PRK08317  86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 67-177 3.76e-23

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 91.71  E-value: 3.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    67 RSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDKLLDKGVSgNVSFVQADAEKLP--FPDNHFDCVTI 144
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFD-NVEFEQGDIEELPelLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15600256   145 AFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFS 177
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 73-173 5.69e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 86.95  E-value: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    73 LDIAGGTGDLTRQFSRLVGptgEVVLADINASMLKVGRDKLLDKGVSgnvsFVQADAEKLPFPDNHFDCVTIAFGLRNVT 152
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKAPREGLT----FVVGDAEDLPFPDNSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 15600256   153 HKDEAIRSMLRVLKPGGRLLV 173
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 66-173 6.61e-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: 85.07  E-value: 6.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  66 VRSGNRVLDIAGGTGDLTRQFSRLvgptG-EVVLADINASMLKVGRDKLLDKgvsgNVSFVQADAEKLPFPDNHFDCVTI 144
Cdd:COG2227  22 LPAGGRVLDVGCGTGRLALALARR----GaDVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLPLEDGSFDLVIC 93

                        90       100
                ....*....|....*....|....*....
gi 15600256 145 AFGLRNVTHKDEAIRSMLRVLKPGGRLLV 173
Cdd:COG2227  94 SEVLEHLPDPAALLRELARLLKPGGLLLL 122
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 100-249 6.93e-19

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 80.89  E-value: 6.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  100 DINASMLKVG--RDKLLDKGVSGNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFS 177
Cdd:PLN02232   4 DFSSEQLAVAatRQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFN 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600256  178 KpSSNLLSKAYDAYSFSLLPLMGKLVTNDSESYRYLAESIRMHPDQETLKAMMVEAGFDRVTYHNMTGGIVA 249
Cdd:PLN02232  84 K-SNQSVTTFMQGWMIDNVVVPVATVYDLAKEYEYLKYSINGYLTGEELETLALEAGFSSACHYEISGGFMG 154
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 34-180 1.45e-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: 81.95  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    34 FHSVAAKYDLMNDLMSGGIHRLWKRftIELSGVRSGNRVLDIAGGTGDLTRQFSRLvGPTGEVVLADINASMLKVGRDKl 113
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLAL--LKEKGIFIPASVLDIGCGTGYLTRALLKR-FPQAEFIALDISAGMLAQAKTK- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600256   114 ldkgVSGNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPS 180
Cdd:TIGR02072  78 ----LSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGT 140
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
71-173 3.11e-18

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 77.17  E-value: 3.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  71 RVLDIAGGTGDLTRQFSRLVgPTGEVVLADINASMLKVGRDKLldkgvsGNVSFVQADAEKLPfPDNHFDCVTIAFGLRN 150
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLD-PPEPFDLVVSNAALHW 75

                        90       100
                ....*....|....*....|...
gi 15600256 151 VTHKDEAIRSMLRVLKPGGRLLV 173
Cdd:COG4106  76 LPDHAALLARLAAALAPGGVLAV 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-173 1.41e-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: 70.54  E-value: 1.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  71 RVLDIAGGTGDLTRQFSRLVGptGEVVLADINASMLKVGRDKLLDKGvSGNVSFVQADAEKLPF-PDNHFD-CVTIAFGL 148
Cdd:cd02440   1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPeADESFDvIISDPPLH 77

                        90       100
                ....*....|....*....|....*
gi 15600256 149 RNVTHKDEAIRSMLRVLKPGGRLLV 173
Cdd:cd02440  78 HLVEDLARFLEEARRLLKPGGVLVL 102
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 58-173 5.57e-15

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 70.34  E-value: 5.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  58 RFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGptGEVVLADINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPfPDN 137
Cdd:COG2230  41 DLILRKLGLKPGMRVLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADG 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15600256 138 HFDCV-----TIAFGLRNVthkDEAIRSMLRVLKPGGRLLV 173
Cdd:COG2230 118 QFDAIvsigmFEHVGPENY---PAYFAKVARLLKPGGRLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 55-226 8.05e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 70.72  E-value: 8.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  55 LWKRFTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGptGEVVLADINASMLKVGRDKLLDKGVsGNVSFVQADAEKL-P 133
Cdd:COG0500  13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELdP 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256 134 FPDNHFDCVTiafgLRNVTH------KDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAYDAYSFSLLPLMGKLVTNDS 207
Cdd:COG0500  90 LPAESFDLVV----AFGVLHhlppeeREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLRLLAL 165

                       170
                ....*....|....*....
gi 15600256 208 ESYRYLAESIRMHPDQETL 226
Cdd:COG0500 166 ELYLRALLAAAATEDLRSD 184
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
30-172 1.55e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 66.95  E-value: 1.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  30 VAEVFHSVAAKYD--LMNDLMSGGIHRLWKRFtIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGptgEVVLADINASMLK 107
Cdd:COG4976   7 VEALFDQYADSYDaaLVEDLGYEAPALLAEEL-LARLPPGPFGRVLDLGCGTGLLGEALRPRGY---RLTGVDLSEEMLA 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600256 108 VGRDKLLDkgvsgnVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLL 172
Cdd:COG4976  83 KAREKGVY------DRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
arsM PRK11873
arsenite methyltransferase;
62-173 4.80e-13

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 66.90  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   62 ELSGVRSGNRVLDIAGGTG-D--LTRqfsRLVGPTGEVVLADINASMLKVGRDKLlDKGVSGNVSFVQADAEKLPFPDNH 138
Cdd:PRK11873  71 ALAELKPGETVLDLGSGGGfDcfLAA---RRVGPTGKVIGVDMTPEMLAKARANA-RKAGYTNVEFRLGEIEALPVADNS 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15600256  139 FD-----CVtiafgLRNVTHKDEAIRSMLRVLKPGGRLLV 173
Cdd:PRK11873 147 VDviisnCV-----INLSPDKERVFKEAFRVLKPGGRFAI 181
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 73-171 1.33e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 62.00  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    73 LDIAGGTGDLTRQFSRLVgPTGEVVLADINASMLKVGRDKLLDKGVsGNVSFVQADAEKLPFPD-NHFDCVTIAFGLRNV 151
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAL-PGLEYTGLDISPAALEAARERLAALGL-LNAVRVELFQLDLGELDpGSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|
gi 15600256   152 THKDEAIRSMLRVLKPGGRL 171
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 63-190 8.16e-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: 63.25  E-value: 8.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  63 LSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDKLLDKGVSGNVSFVQADAEKlPFPDNHFDCV 142
Cdd:COG2519  86 RLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIRE-GIDEGDVDAV 164

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600256 143 TIafglrnvthkD-----EAIRSMLRVLKPGGRLLVLefsKPSSNLLSKAYDA 190
Cdd:COG2519 165 FL----------DmpdpwEALEAVAKALKPGGVLVAY---VPTVNQVSKLVEA 204
PRK05785 PRK05785
hypothetical protein; Provisional
 30-213 3.14e-11

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 61.24  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   30 VAEVFHSVAAKYDLMNDLMSGGIHRLWKRFTIELSGVRSGN--RVLDIAGGTGDLTRQFSRLVgpTGEVVLADINASMLK 107
Cdd:PRK05785  11 LQEAYNKIPKAYDRANRFISFNQDVRWRAELVKTILKYCGRpkKVLDVAAGKGELSYHFKKVF--KYYVVALDYAENMLK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  108 ---VGRDKlldkgvsgnvsfVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKpgGRLLVLEFSKPSSNLL 184
Cdd:PRK05785  89 mnlVADDK------------VVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR--KQVGFIAMGKPDNVIK 154

                        170       180
                 ....*....|....*....|....*....
gi 15600256  185 SKAYDAYSFSLLPLMGKLVTNDSESYRYL 213
Cdd:PRK05785 155 RKYLSFYLRYIMPYIACLAGAKCRDYKYI 183
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-193 8.60e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 58.98  E-value: 8.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    52 IHRLWKRFTIELSGV-RSGNRVLDIAGGTGDLTRQFsRLVGPTGEVVlaDINASMLKVGRDklldkgvsgNVSFVQADAE 130
Cdd:pfam13489   5 RERLLADLLLRLLPKlPSPGRVLDFGCGTGIFLRLL-RAQGFSVTGV--DPSPIAIERALL---------NVRFDQFDEQ 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600256   131 KLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKPSSNLLSKAYDAYSF 193
Cdd:pfam13489  73 EAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLR 135
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
60-175 2.71e-10

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 59.16  E-value: 2.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  60 TIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLA-----DINASMLKVGRDKL-----LDKGVSGNVSFVQADA 129
Cdd:COG4798  58 TLAFFGVKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAAnfdpdSEPPEYAKRSREAFsaklaADPALYGNVRVTAFAP 137

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600256 130 EKLPF-PDNHFDCVTIAfglRNVtH-------KDEAIRSMLRVLKPGGRLLVLE 175
Cdd:COG4798 138 PDDPIaPPGSADLVLTF---RNY-HnwyragdAAAMFAAFFKALKPGGVLGVVD 187
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 58-174 4.99e-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: 54.18  E-value: 4.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  58 RFTIELSGVRSGNRVLDIAGGTGDLTrQFSRLVGPtgEVVLADINASMLKVGRDKLLDKGVsGNVSFVQADAEKLPFPDN 137
Cdd:COG1041  16 RALVNLAGAKEGDTVLDPFCGTGTIL-IEAGLLGR--RVIGSDIDPKMVEGARENLEHYGY-EDADVIRGDARDLPLADE 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15600256 138 HFDCVtIA---FGLRNVTHKDE-------AIRSMLRVLKPGGRLLVL 174
Cdd:COG1041  92 SVDAI-VTdppYGRSSKISGEEllelyekALEEAARVLKPGGRVVIV 137
PLN02244 PLN02244
tocopherol O-methyltransferase
 71-191 6.29e-08

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 52.44  E-value: 6.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   71 RVLDIAGGTGDLTRQFSRLVGPTGE-VVLADINAsmlKVGRDKLLDKGVSGNVSFVQADAEKLPFPDNHFDCVtiaFGLR 149
Cdd:PLN02244 121 RIVDVGCGIGGSSRYLARKYGANVKgITLSPVQA---ARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLV---WSME 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600256  150 NVTH---KDEAIRSMLRVLKPGGRLLV-------LEFSKPS-----SNLLSKAYDAY 191
Cdd:PLN02244 195 SGEHmpdKRKFVQELARVAAPGGRIIIvtwchrdLEPGETSlkpdeQKLLDKICAAY 251
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
62-173 1.49e-07

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.44  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    62 ELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDKLLDKGVSgNVSFVQAD-----AEKLPFPD 136
Cdd:pfam01135  67 ELLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE-NVIVVVGDgrqgwPEFAPYDA 145

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15600256   137 NHfdcVTIAfglrnvthKDEAIRSMLRVLKPGGRLLV 173
Cdd:pfam01135 146 IH---VGAA--------APEIPEALIDQLKEGGRLVI 171
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 30-171 2.00e-07

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 50.53  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   30 VAEVFHSVAAKYDLMNDLMSGGIHRLwkrftIELSGVRSGNRVLDIAGGTGDLTRqFSRLVGptGEVVLADINASMLKVG 109
Cdd:PRK10258   9 IAAAFGRAAAHYEQHAELQRQSADAL-----LAMLPQRKFTHVLDAGCGPGWMSR-YWRERG--SQVTALDLSPPMLAQA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600256  110 RDKlldkgvSGNVSFVQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRL 171
Cdd:PRK10258  81 RQK------DAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVV 136
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
71-195 2.21e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 47.41  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256     71 RVLDIAGGTG----DLTRQFS--RLVGPTgevvladINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFPDNHfdcvTI 144
Cdd:smart00828   2 RVLDFGCGYGsdliDLAERHPhlQLHGYT-------ISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTY----DL 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15600256    145 AFGLRNVTH---KDEAIRSMLRVLKPGGRLLVLEF-SKPSSNLLSKAYDAYSFSL 195
Cdd:smart00828  71 VFGFEVIHHikdKMDLFSNISRHLKDGGHLVLADFiANLLSAIEHEETTSYLVTR 125
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
71-171 3.02e-06

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 47.27  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   71 RVLDIAGGTGDLTRQFSRLvgptG-EVVLADINASMLKVGRDKLLDKGVSGNVSFVQADAEKL-PFPDNHFDCVTIAFGL 148
Cdd:PRK11036  47 RVLDAGGGEGQTAIKLAEL----GhQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIaQHLETPVDLILFHAVL 122

                         90       100
                 ....*....|....*....|...
gi 15600256  149 RNVTHKDEAIRSMLRVLKPGGRL 171
Cdd:PRK11036 123 EWVADPKSVLQTLWSVLRPGGAL 145
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
63-142 7.03e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.67  E-value: 7.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  63 LSGVRSGNRVLDIAGGTGDLTRqFSRLVGPTgEVVLADINASMLKVGRDKLLDKGVsgNVSFVQADAEKLPfPDNHFDCV 142
Cdd:COG2263  40 LRGDIEGKTVLDLGCGTGMLAI-GAALLGAK-KVVGVDIDPEALEIARENAERLGV--RVDFIRADVTRIP-LGGSVDTV 114
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 71-170 1.23e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 45.65  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   71 RVLDIAGGTGDLTRQFSRLVGPtGEVVLADINASMLKVGRDKLLDKGVSgnvsFVQADAEKLPFPDNHFDCVTIAFGLRN 150
Cdd:PLN02490 116 KVVDVGGGTGFTTLGIVKHVDA-KNVTILDQSPHQLAKAKQKEPLKECK----IIEGDAEDLPFPTDYADRYVSAGSIEY 190

                         90       100
                 ....*....|....*....|
gi 15600256  151 VTHKDEAIRSMLRVLKPGGR 170
Cdd:PLN02490 191 WPDPQRGIKEAYRVLKIGGK 210
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 61-173 3.74e-05

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 44.07  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   61 IELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDKLLDKGVSgNVSFVQADAEKLPFPDNHFD 140
Cdd:PRK13943  73 MEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGIE-NVIFVCGDGYYGVPEFAPYD 151

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15600256  141 CVTIAFGLrnvthkDEAIRSMLRVLKPGGRLLV 173
Cdd:PRK13943 152 VIFVTVGV------DEVPETWFTQLKEGGRVIV 178
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 66-171 4.22e-05

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: 43.63  E-value: 4.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    66 VRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFP---DNHFDCV 142
Cdd:pfam08704  38 LRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADKAREEFREHGIDQLVTVTHRDVCKEGFLtevSGKADAV 117

                          90       100       110
                  ....*....|....*....|....*....|
gi 15600256   143 TIafglrNVTHKDEAIRSMLRVLK-PGGRL 171
Cdd:pfam08704 118 FL-----DLPSPWEAVPHAWKALKvEGGRF 142
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 49-191 4.60e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 43.97  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   49 SGGIHRLwKRFTIELSgVRSGNRVLD----IAGGTGDLTRQFSRlvgptgEVVLADINASMLKVGRDKLLdkGVSGNVSF 124
Cdd:PLN02336 249 TGGLETT-KEFVDKLD-LKPGQKVLDvgcgIGGGDFYMAENFDV------HVVGIDLSVNMISFALERAI--GRKCSVEF 318

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600256  125 VQADAEKLPFPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVLKPGGRLLVLEFSKpSSNLLSKAYDAY 191
Cdd:PLN02336 319 EVADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCR-SPGTPSPEFAEY 384
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 59-176 7.38e-05

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


Pssm-ID: 399779  Cd Length: 193  Bit Score: 42.44  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    59 FTIELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPTG---EVVLADINASMLKvgrdklldkgvsgNVSFVQADAEK--LP 133
Cdd:pfam07021   4 FRYILEWIPPGSRVLDLGCGDGTLLYLLKEEKGVDGygiELDAAGVAECVAK-------------GLYVIQGDLDEglEH 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 15600256   134 FPDNHFDCVTIAFGLRNVTHKDEAIRSMLRVlkpgGRLLVLEF 176
Cdd:pfam07021  71 FPDKSFDYVILSQTLQATRNPREVLDEMLRI----GRRCIVSF 109
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 69-173 8.62e-05

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 42.10  E-value: 8.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  69 GNRVLDIAGGTGDLTRQFSRLvGPTGEVVLADINASMLKVGRDKLLDKGVSgNVSFVQADAEKlPFPDNHFDCVtiafgL 148
Cdd:COG2813  50 GGRVLDLGCGYGVIGLALAKR-NPEARVTLVDVNARAVELARANAAANGLE-NVEVLWSDGLS-GVPDGSFDLI-----L 121

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15600256 149 RN------VTHKDEAIRSML----RVLKPGGRLLV 173
Cdd:COG2813 122 SNppfhagRAVDKEVAHALIadaaRHLRPGGELWL 156
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 61-173 1.03e-04

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 42.00  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  61 IELSGVRSGNRVLDIAGGTGDLTRQFSRLVgptGEVVLADINASMLKVGRDKLLDKGVSgNVSFVQADAEkLPFPDNH-F 139
Cdd:COG2518  59 LEALDLKPGDRVLEIGTGSGYQAAVLARLA---GRVYSVERDPELAERARERLAALGYD-NVTVRVGDGA-LGWPEHApF 133

                        90       100       110
                ....*....|....*....|....*....|....
gi 15600256 140 DCVTIAFGLRNVThkdeaiRSMLRVLKPGGRLLV 173
Cdd:COG2518 134 DRIIVTAAAPEVP------EALLEQLAPGGRLVA 161
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
66-172 1.29e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 41.95  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  66 VRSGNRVLDIAGGTGDLTRQFSRLvgPTGEVVLADINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFPdNHFDcVTIA 145
Cdd:COG4076  33 VKPGDVVLDIGTGSGLLSMLAARA--GAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLP-EKAD-VIIS 108

                        90       100       110
                ....*....|....*....|....*....|.
gi 15600256 146 FGLRNVTHKDEAIRSML----RVLKPGGRLL 172
Cdd:COG4076 109 EMLDTALLDEGQVPILNharkRLLKPGGRII 139
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 66-173 1.94e-04

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 41.32  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   66 VRSGNRVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDKLLDKGVSGNVSFVQADA-EKLPFPDNHFDCVTI 144
Cdd:PRK00377  38 LRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEApEILFTINEKFDRIFI 117

                         90       100
                 ....*....|....*....|....*....
gi 15600256  145 AFGLRNVthkDEAIRSMLRVLKPGGRLLV 173
Cdd:PRK00377 118 GGGSEKL---KEIISASWEIIKKGGRIVI 143
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 18-174 6.71e-04

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: 40.00  E-value: 6.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  18 YQNVPESQKAKKVAEVFHSVAAkydLMNDLMSGGIHRLwkrftIELSGVRSGNRVLDI-AGGTGDLTRQFSRLVGptGEV 96
Cdd:cd05188  92 YVVVPADNLVPLPDGLSLEEAA---LLPEPLATAYHAL-----RRAGVLKPGDTVLVLgAGGVGLLAAQLAKAAG--ARV 161

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600256  97 VLADINASMLKVGRDKLLDKGVsgNVSFVQADAEKLPFPDNHFDCVTIAFGlrnvthKDEAIRSMLRVLKPGGRLLVL 174
Cdd:cd05188 162 IVTDRSDEKLELAKELGADHVI--DYKEEDLEEELRLTGGGGADVVIDAVG------GPETLAQALRLLRPGGRIVVV 231
rADc smart00650
Ribosomal RNA adenine dimethylases;
61-142 8.67e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 8.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256     61 IELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPtgeVVLADINASMLKVGRDKLLDkgvSGNVSFVQADAEKLPFPDNHFD 140
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGALTEELLERAKR---VTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKLQPY 79


                   ..
gi 15600256    141 CV 142
Cdd:smart00650  80 KV 81
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 71-175 2.58e-03

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


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 38.40  E-value: 2.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256  71 RVLDIAGGTGDLTRQFSRLVGPTGEVVLADINASMLKVGRDkLLDKGVSGNVSFVQADAEKL--PFPDNHFDCVTIAfgl 148
Cdd:COG5459  83 TVLDVGAGPGTAAWAAADAWPSLLDATLLERSAAALALGRR-LARAAANPALETAEWRLADLaaALPAPPADLVVAS--- 158

                        90       100       110
                ....*....|....*....|....*....|...
gi 15600256 149 rNV------THKDEAIRSMLrvLKPGGRLLVLE 175
Cdd:COG5459 159 -YVlneladAARAALVDRLW--LAPDGALLIVE 188
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 69-173 3.04e-03

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 37.57  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256    69 GNRVLDIAGGTGDLTRQFSRLvGPTGEVVLADINASMLKVGRDKLLDKGVSgNVSFVQADAEKlPFPDNHFDCVT----I 144
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKE-SPDAELTMVDINARALESARENLAANGLE-NGEVVASDVYS-GVEDGKFDLIIsnppF 108

                          90       100       110
                  ....*....|....*....|....*....|..
gi 15600256   145 AFGL---RNVTHkdEAIRSMLRVLKPGGRLLV 173
Cdd:pfam05175 109 HAGLattYNVAQ--RFIADAKRHLRPGGELWI 138
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 61-142 3.83e-03

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 38.06  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   61 IELSGVRSGNRVLDIAGGTGDLTrqfSRLVGPTGEVVLADINASMLKVGRDKLLDKGVSGNVSFVQADAEKLPFPDnhFD 140
Cdd:PTZ00338  29 VEKAAIKPTDTVLEIGPGTGNLT---EKLLQLAKKVIAIEIDPRMVAELKKRFQNSPLASKLEVIEGDALKTEFPY--FD 103


                 ...
gi 15600256  141 -CV 142
Cdd:PTZ00338 104 vCV 106
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
61-142 5.67e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 37.19  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600256   61 IELSGVRSGNRVLDIAGGTGDLTRQFSRLVGPtgeVVLADINASMLKVGRDKLLDkgvSGNVSFVQADAEKLPFPDnhFD 140
Cdd:PRK14896  22 VEYAEDTDGDPVLEIGPGKGALTDELAKRAKK---VYAIELDPRLAEFLRDDEIA---AGNVEIIEGDALKVDLPE--FN 93


                 ..
gi 15600256  141 CV 142
Cdd:PRK14896  94 KV 95
 
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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