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Conserved domains on  [gi|25143945|ref|NP_497549|]
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Sterol 4-C-methyltransferase strm-1 [Caenorhabditis elegans]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 86-207 4.44e-30

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: 111.62  E-value: 4.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  86 HIAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGIsdRCKIVAADCQKMPFEDSTFDV 165
Cdd:COG2226  13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGSFDL 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 25143945 166 AYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYDLIKTNDYD 207
Cdd:COG2226  91 VISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 86-207 4.44e-30

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: 111.62  E-value: 4.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  86 HIAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGIsdRCKIVAADCQKMPFEDSTFDV 165
Cdd:COG2226  13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGSFDL 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 25143945 166 AYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYDLIKTNDYD 207
Cdd:COG2226  91 VISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 100-197 7.75e-26

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 98.89  E-value: 7.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGISDRCkivaADCQKMPFEDSTFDVAYAIYSLKYIPNLD 179
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVV----GDAEDLPFPDNSFDLVLSSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 25143945   180 KVMKEIQRVLKPGGKFIV 197
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 89-197 7.43e-20

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 86.75  E-value: 7.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   89 EKLELSENVHCLDIGCGIGGVMLDIADFG---AKLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQKMPFEDSTFDv 165
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFD- 123

                         90       100       110
                 ....*....|....*....|....*....|...
gi 25143945  166 AYAI-YSLKYIPNLDKVMKEIQRVLKPGGKFIV 197
Cdd:PRK00216 124 AVTIaFGLRNVPDIDKALREMYRVLKPGGRLVI 156
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 88-204 1.82e-18

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: 82.70  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945    88 AEKLELSENVHCLDIGCGIGGVMLDIADFG---AKLTGVTIAPNEAEIGNEKFANMgisDRCKIVAADCQKMPFEDSTFD 164
Cdd:TIGR01934  32 VKLIGVFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSELP---LNIEFIQADAEALPFEDNSFD 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 25143945   165 VAYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYDLIKTN 204
Cdd:TIGR01934 109 AVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPA 148
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
98-201 1.88e-12

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 65.90  E-value: 1.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945     98 HCLDIGCGIGGVMLDIADFGA--KLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQKMPFEDsTFDVAYAIYSLKYI 175
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPD-TYDLVFGFEVIHHI 80

                           90       100
                   ....*....|....*....|....*.
gi 25143945    176 PNLDKVMKEIQRVLKPGGKFIVYDLI 201
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFI 106
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 100-197 1.85e-11

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: 60.14  E-value: 1.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945 100 LDIGCGIGGVMLDIADF-GAKLTGVTIAPNEAEIGnEKFANMGISDRCKIVAADCQKMPF-EDSTFDVAYAIYSLKYIP- 176
Cdd:cd02440   3 LDLGCGTGALALALASGpGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLVe 81

                        90       100
                ....*....|....*....|.
gi 25143945 177 NLDKVMKEIQRVLKPGGKFIV 197
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 86-207 4.44e-30

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: 111.62  E-value: 4.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  86 HIAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGIsdRCKIVAADCQKMPFEDSTFDV 165
Cdd:COG2226  13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGSFDL 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 25143945 166 AYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYDLIKTNDYD 207
Cdd:COG2226  91 VISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 100-197 7.75e-26

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 98.89  E-value: 7.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGISDRCkivaADCQKMPFEDSTFDVAYAIYSLKYIPNLD 179
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVV----GDAEDLPFPDNSFDLVLSSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 25143945   180 KVMKEIQRVLKPGGKFIV 197
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 76-199 3.69e-24

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 96.54  E-value: 3.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  76 LEEALKSLHCHIAEKLELSENVHCLDIGCGIGGVMLDIAD-FGAKLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQ 154
Cdd:COG2230  32 LEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYR 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 25143945 155 KMPFEDStFDVAYAIYSLKYIP--NLDKVMKEIQRVLKPGGKFIVYD 199
Cdd:COG2230 112 DLPADGQ-FDAIVSIGMFEHVGpeNYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 100-193 3.96e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 94.17  E-value: 3.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGIGGVMLDIAD-FGAKLTGVTIAPNEAEIGNEKFANMGIsdRCKIVAADCQKMPFEDSTFDVAYAIYSLKYI--P 176
Cdd:pfam13649   2 LDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdP 79

                          90
                  ....*....|....*..
gi 25143945   177 NLDKVMKEIQRVLKPGG 193
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 100-197 2.13e-20

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 85.45  E-value: 2.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945 100 LDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGISdrckIVAADCQKMPFEDSTFDVAYAIYSLKYIPNLD 179
Cdd:COG2227  29 LDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD----FVQGDLEDLPLEDGSFDLVICSEVLEHLPDPA 104

                        90
                ....*....|....*...
gi 25143945 180 KVMKEIQRVLKPGGKFIV 197
Cdd:COG2227 105 ALLRELARLLKPGGLLLL 122
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 89-197 7.43e-20

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 86.75  E-value: 7.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   89 EKLELSENVHCLDIGCGIGGVMLDIADFG---AKLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQKMPFEDSTFDv 165
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFD- 123

                         90       100       110
                 ....*....|....*....|....*....|...
gi 25143945  166 AYAI-YSLKYIPNLDKVMKEIQRVLKPGGKFIV 197
Cdd:PRK00216 124 AVTIaFGLRNVPDIDKALREMYRVLKPGGRLVI 156
PLN02244 PLN02244
tocopherol O-methyltransferase
 100-197 1.56e-19

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 87.88  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  100 LDIGCGIGGVMLDIAD-FGAKLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQKMPFEDSTFDVAYAIYSLKYIPNL 178
Cdd:PLN02244 123 VDVGCGIGGSSRYLARkYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDK 202

                         90
                 ....*....|....*....
gi 25143945  179 DKVMKEIQRVLKPGGKFIV 197
Cdd:PLN02244 203 RKFVQELARVAAPGGRIII 221
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 88-204 1.82e-18

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: 82.70  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945    88 AEKLELSENVHCLDIGCGIGGVMLDIADFG---AKLTGVTIAPNEAEIGNEKFANMgisDRCKIVAADCQKMPFEDSTFD 164
Cdd:TIGR01934  32 VKLIGVFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSELP---LNIEFIQADAEALPFEDNSFD 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 25143945   165 VAYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYDLIKTN 204
Cdd:TIGR01934 109 AVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPA 148
PRK08317 PRK08317
hypothetical protein; Provisional
 86-199 5.40e-18

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 81.91  E-value: 5.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   86 HIAEKLELSENVHCLDIGCGIGGVMLDIADF---GAKLTGVTIAPNEAEIGNEKFANMGisDRCKIVAADCQKMPFEDST 162
Cdd:PRK08317  10 RTFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADGLPFPDGS 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 25143945  163 FDVAYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYD 199
Cdd:PRK08317  88 FDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 93-199 7.48e-14

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 68.21  E-value: 7.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945    93 LSENVHCLDIGCGIGGVMLDIAD---FGAKLTGVTIAPNEAEIGNEKFANMGIsDRCKIVAADCQKMP--FEDSTFDVAY 167
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPelLEDDKFDVVI 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 25143945   168 AIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYD 199
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISD 111
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
78-196 7.96e-14

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 68.87  E-value: 7.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  78 EALKSLHCHIAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKfanmGISDRckIVAADCQKMP 157
Cdd:COG4976  29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK----GVYDR--LLVADLADLA 102

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 25143945 158 FEDSTFDVAYAIYSLKYIPNLDKVMKEIQRVLKPGGKFI 196
Cdd:COG4976 103 EPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
100-197 1.39e-13

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 69.01  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGIGGVMLDIADF---GAKLTGVTIAPNEAEIGNEKFANMGISDrCKIVAADCQKMPFEDSTFDVAYAIYSLKYIP 176
Cdd:pfam01209  47 LDVAGGTGDWTFGLSDSagsSGKVVGLDINENMLKEGEKKAKEEGKYN-IEFLQGNAEELPFEDDSFDIVTISFGLRNFP 125

                          90       100
                  ....*....|....*....|.
gi 25143945   177 NLDKVMKEIQRVLKPGGKFIV 197
Cdd:pfam01209 126 DYLKVLKEAFRVLKPGGRVVC 146
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
98-197 7.48e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 63.69  E-value: 7.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  98 HCLDIGCGIGGVMLDIAD--FGAKLTGVTIAPNEAEIGNEKFANmgisdrCKIVAADCQKMPFEDStFDVAYAIYSLKYI 175
Cdd:COG4106   4 RVLDLGCGTGRLTALLAErfPGARVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEP-FDLVVSNAALHWL 76

                        90       100
                ....*....|....*....|..
gi 25143945 176 PNLDKVMKEIQRVLKPGGKFIV 197
Cdd:COG4106  77 PDHAALLARLAAALAPGGVLAV 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 77-197 1.46e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 65.71  E-value: 1.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  77 EEALKSLHCHIAEKLELSENVHCLDIGCGIGGVMLDIAD-FGAKLTGVTIAPnEA-EIGNEKFANMGISdRCKIVAADCQ 154
Cdd:COG0500   8 DELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAArFGGRVIGIDLSP-EAiALARARAAKAGLG-NVEFLVADLA 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 25143945 155 K-MPFEDSTFDVAYAIYSLKYIP--NLDKVMKEIQRVLKPGGKFIV 197
Cdd:COG0500  86 ElDPLPAESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLL 131
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
98-201 1.88e-12

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 65.90  E-value: 1.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945     98 HCLDIGCGIGGVMLDIADFGA--KLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQKMPFEDsTFDVAYAIYSLKYI 175
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPD-TYDLVFGFEVIHHI 80

                           90       100
                   ....*....|....*....|....*.
gi 25143945    176 PNLDKVMKEIQRVLKPGGKFIVYDLI 201
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFI 106
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 100-195 3.23e-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: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGIGGVMLDIADF--GAKLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQKMPFEDSTFDVAYAIYSLKYIPN 177
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 25143945   178 LDKVMKEIQRVLKPGGKF 195
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 100-197 1.85e-11

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: 60.14  E-value: 1.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945 100 LDIGCGIGGVMLDIADF-GAKLTGVTIAPNEAEIGnEKFANMGISDRCKIVAADCQKMPF-EDSTFDVAYAIYSLKYIP- 176
Cdd:cd02440   3 LDLGCGTGALALALASGpGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLVe 81

                        90       100
                ....*....|....*....|.
gi 25143945 177 NLDKVMKEIQRVLKPGGKFIV 197
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVL 102
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 76-197 7.33e-10

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 58.88  E-value: 7.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945    76 LEEALKSLHCHIAEKLELSENVHCLDIGCGIGGVMLD-IADFGAKLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQ 154
Cdd:pfam02353  42 LEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRaAERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYR 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 25143945   155 KMpfeDSTFDvayAIYSLKYIP-----NLDKVMKEIQRVLKPGGKFIV 197
Cdd:pfam02353 122 DF---DEPFD---RIVSVGMFEhvgheNYDTFFKKLYNLLPPGGLMLL 163
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 87-242 7.96e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 57.05  E-value: 7.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945    87 IAEKLELSENVhcLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFanmgisdrcKIVAADCQKMPFEDSTFDVA 166
Cdd:pfam13489  16 LLPKLPSPGRV--LDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNV---------RFDQFDEQEAAVPAGKFDVI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25143945   167 YAIYSLKYIPNLDKVMKEIQRVLKPGGKFivydLIKTNDYDKDNKEHYKTLHHLEYACGMPSLHTQSEVEAAAEKW 242
Cdd:pfam13489  85 VAREVLEHVPDPPALLRQIAALLKPGGLL----LLSTPLASDEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEA 156
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 87-215 2.37e-09

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 57.29  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   87 IAEKLELSENVHCLDIGCGIGGVMLDIAD-FGAKLTGVTIAPNEAEIGNEKfanmgISDRCKIV--AADCQKMPFEDSTF 163
Cdd:PTZ00098  44 ILSDIELNENSKVLDIGSGLGGGCKYINEkYGAHVHGVDICEKMVNIAKLR-----NSDKNKIEfeANDILKKDFPENTF 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143945  164 DVAYAIYSLKYIPNLDKVM--KEIQRVLKPGGKFIVYDLI--KTNDYDKDNKEHYK 215
Cdd:PTZ00098 119 DMIYSRDAILHLSYADKKKlfEKCYKWLKPNGILLITDYCadKIENWDEEFKAYIK 174
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 89-214 3.05e-09

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 57.84  E-value: 3.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   89 EKLELSENVHCLDIGCGIGGVMLDIA-DFGAKLTGVTIAPNEAEIGNEKfanmGISDRCKIV--AADCQKMPFEDSTFDV 165
Cdd:PLN02336 260 DKLDLKPGQKVLDVGCGIGGGDFYMAeNFDVHVVGIDLSVNMISFALER----AIGRKCSVEfeVADCTKKTYPDNSFDV 335

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25143945  166 AYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYD--------------LIKTNDYDKDNKEHY 214
Cdd:PLN02336 336 IYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDycrspgtpspefaeYIKQRGYDLHDVQAY 398
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 100-256 1.31e-07

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: 51.90  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGIGGVMLDIADFG--AKLTGVTIAPNEaeignEKFANMGISDRCKIVAADCQKMPFEDSTFDVAYAIYSLKYIPN 177
Cdd:TIGR02072  39 LDIGCGTGYLTRALLKRFpqAEFIALDISAGM-----LAQAKTKLSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDD 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   178 LDKVMKEIQRVLKPGGKFIVYDLIKtndydkdnkehyKTLHHLEYACGMPSLH--TQSEVEAA-AEKWEMPVVERENLEE 254
Cdd:TIGR02072 114 LSQALSELARVLKPGGLLAFSTFGP------------GTLHELRQSFGQHGLRylSLDELKALlKNSFELLTLEEELITL 181


                  ..
gi 25143945   255 TY 256
Cdd:TIGR02072 182 SF 183
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 100-198 3.16e-07

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: 49.56  E-value: 3.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945 100 LDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGISDrCKIVAADCQKMPFEDSTFDVA-----YAIYSLKY 174
Cdd:COG1041  31 LDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADESVDAIvtdppYGRSSKIS 109

                        90       100
                ....*....|....*....|....*...
gi 25143945 175 IPNLD----KVMKEIQRVLKPGGKFIVY 198
Cdd:COG1041 110 GEELLelyeKALEEAARVLKPGGRVVIV 137
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 98-197 1.13e-06

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 48.99  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945  98 HCLDIGCGIGGVMLDIAD--FGAKLTGVTIAPNEAEIGNEKFANMGISDRCKIVAADCQKMP--FEDSTFDVA------Y 167
Cdd:COG4123  40 RVLDLGTGTGVIALMLAQrsPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaeLPPGSFDLVvsnppyF 119

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 25143945 168 AIYSLKYIPN-------------LDKVMKEIQRVLKPGGKFIV 197
Cdd:COG4123 120 KAGSGRKSPDearaiarhedaltLEDLIRAAARLLKPGGRFAL 162
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 98-194 1.99e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 48.22  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   98 HCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFAnmgiSDRckIVAADCQKMPFEDSTFDVAYAIYSLKYIPN 177
Cdd:PRK10258  45 HVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDA----ADH--YLAGDIESLPLATATFDLAWSNLAVQWCGN 118

                         90
                 ....*....|....*..
gi 25143945  178 LDKVMKEIQRVLKPGGK 194
Cdd:PRK10258 119 LSTALRELYRVVRPGGV 135
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
72-195 2.79e-06

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 48.69  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   72 EGQKLEEA-LKSLHChIAEKLELSENVHCLDIGCGIGGVMLDIAD-FGAKLTGVTIAPNEAEIGNEKfanmgisdrckiv 149
Cdd:PRK11705 144 DADTLEEAqEAKLDL-ICRKLQLKPGMRVLDIGCGWGGLARYAAEhYGVSVVGVTISAEQQKLAQER------------- 209

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25143945  150 aadCQKMPFE---------DSTFDvayAIYSL--------KyipNLDKVMKEIQRVLKPGGKF 195
Cdd:PRK11705 210 ---CAGLPVEirlqdyrdlNGQFD---RIVSVgmfehvgpK---NYRTYFEVVRRCLKPDGLF 263
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 48-194 4.12e-06

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 47.96  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   48 YYSVMSTVIDeyfggnfHFVPPKFEGQKL-EEALkslhchiaEKLELSE-NVHCLDIGCGIGGVMLDIADFgAKLTGVTI 125
Cdd:PLN02490  79 FYRFLSIVYD-------HIINPGHWTEDMrDDAL--------EPADLSDrNLKVVDVGGGTGFTTLGIVKH-VDAKNVTI 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25143945  126 ---APNEAEIGNEKFANMGisdrCKIVAADCQKMPFEDSTFDVAYAIYSLKYIPNLDKVMKEIQRVLKPGGK 194
Cdd:PLN02490 143 ldqSPHQLAKAKQKEPLKE----CKIIEGDAEDLPFPTDYADRYVSAGSIEYWPDPQRGIKEAYRVLKIGGK 210
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 149-204 4.33e-06

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 47.58  E-value: 4.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143945  149 VAADCQKMPFEDSTFDVAYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYDLIKTN 204
Cdd:PLN02233 132 IEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKST 187
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 149-204 1.38e-05

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 44.68  E-value: 1.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143945  149 VAADCQKMPFEDSTFDVAYAIYSLKYIPNLDKVMKEIQRVLKPGGKFIVYDLIKTN 204
Cdd:PLN02232  31 IEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFNKSN 86
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 100-197 4.27e-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: 44.21  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGiGGVMLD-IADFGAKLTGVTIAPNEAEIGNE--KFANMGISDRCKIVAADCQKmpfEDSTFDVAYAIYSLKYIP 176
Cdd:TIGR01983  51 LDVGCG-GGLLSEpLARLGANVTGIDASEENIEVAKLhaKKDPLQIDYRCTTVEDLAEK---KAGSFDVVTCMEVLEHVP 126

                          90       100
                  ....*....|....*....|.
gi 25143945   177 NLDKVMKEIQRVLKPGGKFIV 197
Cdd:TIGR01983 127 DPQAFIRACAQLLKPGGILFF 147
arsM PRK11873
arsenite methyltransferase;
152-201 4.49e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 44.17  E-value: 4.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 25143945  152 DCQKMPFEDSTFDVayaIYS---LKYIPNLDKVMKEIQRVLKPGGKFIVYDLI 201
Cdd:PRK11873 136 EIEALPVADNSVDV---IISncvINLSPDKERVFKEAFRVLKPGGRFAISDVV 185
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
148-197 7.44e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 42.55  E-value: 7.44e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25143945 148 IVAADCQKMPFEDSTFDvayAIYS------LkYIPNLDKVMKEIQRVLKPGGKFIV 197
Cdd:COG4627  32 IVGDLTDPLPFPDNSVD---AIYSshvlehL-DYEEAPLALKECYRVLKPGGILRI 83
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 86-196 1.31e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 42.98  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   86 HIAEKLElSENVHCLDIGCGIGGVMLDIAD-----FGAKLTGVTIAPNEAEIGNEKFANmgisdrCKIVAADCQKMPFED 160
Cdd:PRK11088  77 LLAERLD-EKATALLDIGCGEGYYTHALADalpeiTTMQLFGLDISKVAIKYAAKRYPQ------VTFCVASSHRLPFAD 149

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 25143945  161 STFDVAYAIYSlkyiPNLDkvmKEIQRVLKPGGKFI 196
Cdd:PRK11088 150 QSLDAIIRIYA----PCKA---EELARVVKPGGIVI 178
PRK14968 PRK14968
putative methyltransferase; Provisional
 87-198 2.10e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   87 IAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANMGISDRC-KIVAADCQKmPFEDSTFDV 165
Cdd:PRK14968  15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGvEVIRSDLFE-PFRGDKFDV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 25143945  166 ayAIYSLKYIPN-----------------------LDKVMKEIQRVLKPGGK-FIVY 198
Cdd:PRK14968  94 --ILFNPPYLPTeeeeewddwlnyalsggkdgrevIDRFLDEVGRYLKPGGRiLLLQ 148
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 87-174 7.26e-04

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


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 40.68  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945    87 IAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFanmGISDRCKIVAADCQKMPFEDSTFDVA 166
Cdd:TIGR00755  21 IVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLL---SLYNNLEIIEGDALKFDLNELAKDLT 97


                  ....*...
gi 25143945   167 YAIYSLKY 174
Cdd:TIGR00755  98 KVVGNLPY 105
Methyltransf_29 pfam03141
Putative S-adenosyl-L-methionine-dependent methyltransferase; This family is a putative ...
 100-220 1.55e-03

Putative S-adenosyl-L-methionine-dependent methyltransferase; This family is a putative S-adenosyl-L-methionine (SAM)-dependent methyltransferase.


Pssm-ID: 335237 [Multi-domain]  Cd Length: 506  Bit Score: 39.98  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   100 LDIGCGIggvmldiADFGAKL-----TGVTIAPN---EAEIgneKFA-NMGISDRCKIVAAdcQKMPFEDSTFDVAYAiy 170
Cdd:pfam03141 122 LDVGCGV-------ASFGAYLlsrdvLTMSFAPKdvhEAQV---QFAlERGIPAMLGVLGT--KRLPYPSRSFDLAHC-- 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 25143945   171 SLKYIP---NLDKVMKEIQRVLKPGGKFI-----VYdliktNDYDKDNKEHYKTLHHL 220
Cdd:pfam03141 188 SRCRIPwtaNDGILLLEVDRVLRPGGYFVlsgppVY-----ARTEEDLQEIWKEMEDL 240
rADc smart00650
Ribosomal RNA adenine dimethylases;
87-165 1.73e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.65  E-value: 1.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25143945     87 IAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANmgiSDRCKIVAADCQKMPFEDSTFDV 165
Cdd:smart00650   5 IVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAA---ADNLTVIHGDALKFDLPKLQPYK 80
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
87-171 2.01e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 39.11  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25143945   87 IAEKLELSENVHCLDIGCGIGGVMLDIADFGAKLTGVTIAPNEAEIGNEKFANmgiSDRCKIVAADCQKMPFEDSTFDVA 166
Cdd:PRK14896  21 IVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIA---AGNVEIIEGDALKVDLPEFNKVVS 97


                 ....*...
gi 25143945  167 ---YAIYS 171
Cdd:PRK14896  98 nlpYQISS 105
PRK05785 PRK05785
hypothetical protein; Provisional
 154-188 5.28e-03

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 37.74  E-value: 5.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 25143945  154 QKMPFEDSTFDVAYAIYSLKYIPNLDKVMKEIQRV 188
Cdd:PRK05785 102 EALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRV 136
 
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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