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Conserved domains on  [gi|1125442093|gb|OLD69399|]
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MAG: hypothetical protein AUF63_00685 [Candidatus Rokubacteria bacterium 13_1_20CM_70_15]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 78-186 5.69e-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: 82.76  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  78 PRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKhhssGSAPNLSFHHLDIARDELPGaGTFDVLVSMHTL 157
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER----AAELNVDFVQGDLEDLPLED-GSFDLVICSEVL 97

                          90       100
                  ....*....|....*....|....*....
gi 1125442093 158 YWHPDPAALLAASRRALKPGGHAIFLTYN 186
Cdd:COG2227    98 EHLPDPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 78-186 5.69e-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: 82.76  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  78 PRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKhhssGSAPNLSFHHLDIARDELPGaGTFDVLVSMHTL 157
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER----AAELNVDFVQGDLEDLPLED-GSFDLVICSEVL 97

                          90       100
                  ....*....|....*....|....*....
gi 1125442093 158 YWHPDPAALLAASRRALKPGGHAIFLTYN 186
Cdd:COG2227    98 EHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 83-163 7.10e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.06  E-value: 7.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  83 ILDIACGIGNVGLRLARR-GYTVVAVDAVRHLIAIAREKHHSSGsaPNLSFHHLDIARDELPGaGTFDVLVSMHTLYWHP 161
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAG--LNVEFVQGDAEDLPFPD-GSFDLVVSSGVLHHLP 77


                  ..
gi 1125442093 162 DP 163
Cdd:pfam13649  78 DP 79
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 54-187 4.91e-13

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: 66.55  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  54 FGPYESM----IEEIIALVTRSIPvtANPRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREkhHSSGSAPN 129
Cdd:TIGR01983  19 FKPLHKMnplrLDYIRDRIRKNFK--NPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEENIEVAKL--HAKKDPLQ 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1125442093 130 LSFHHLDIARDELPGAGTFDVLVSMHTLYWHPDPAALLAASRRALKPGGHAIFLTYNR 187
Cdd:TIGR01983  95 IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 72-163 1.48e-11

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 62.55  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  72 IPVTANPRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHHSSGSAPNLSFHHLDIArdelPGAGTFDVL 151
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLE----SLLGRFDTV 131

                          90
                  ....*....|..
gi 1125442093 152 VSMHTLYWHPDP 163
Cdd:PRK07580  132 VCLDVLIHYPQE 143
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 82-182 2.96e-08

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: 50.51  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  82 KILDIACGIGNVGLRLARR-GYTVVAVDAVRHLIAIAREKHHSSGsAPNLSFHHLDIARDELPGAGTFDVLVSMHTL-YW 159
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPEADESFDVIISDPPLhHL 79

                          90       100
                  ....*....|....*....|...
gi 1125442093 160 HPDPAALLAASRRALKPGGHAIF 182
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVL 102
rADc smart00650
Ribosomal RNA adenine dimethylases;
68-153 1.87e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 40.96  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093   68 VTRSIPVTANPR-SVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKhhsSGSAPNLSFHHLDIARDELPgAG 146
Cdd:smart00650   1 VIDKIVRAANLRpGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREK---FAAADNLTVIHGDALKFDLP-KL 76


                   ....*..
gi 1125442093  147 TFDVLVS 153
Cdd:smart00650  77 QPYKVVG 83
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 78-186 5.69e-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: 82.76  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  78 PRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKhhssGSAPNLSFHHLDIARDELPGaGTFDVLVSMHTL 157
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER----AAELNVDFVQGDLEDLPLED-GSFDLVICSEVL 97

                          90       100
                  ....*....|....*....|....*....
gi 1125442093 158 YWHPDPAALLAASRRALKPGGHAIFLTYN 186
Cdd:COG2227    98 EHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 47-198 7.43e-19

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: 80.42  E-value: 7.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  47 YDAVVTRFGPYESMIEEIialvtrsipvtANPRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHHSSGs 126
Cdd:COG2226     1 FDRVAARYDGREALLAAL-----------GLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAG- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125442093 127 aPNLSFHHLDIARDELPgAGTFDVLVSMHTLYWHPDPAALLAASRRALKPGGHAIFLTYNRP--ARVVQTFREA 198
Cdd:COG2226    69 -LNVEFVVGDAEDLPFP-DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPdlAELEELLAEA 140
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 83-163 7.10e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.06  E-value: 7.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  83 ILDIACGIGNVGLRLARR-GYTVVAVDAVRHLIAIAREKHHSSGsaPNLSFHHLDIARDELPGaGTFDVLVSMHTLYWHP 161
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAG--LNVEFVQGDAEDLPFPD-GSFDLVVSSGVLHHLP 77


                  ..
gi 1125442093 162 DP 163
Cdd:pfam13649  78 DP 79
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
83-182 9.71e-16

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 71.01  E-value: 9.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  83 ILDIACGIGNVGLRLARR--GYTVVAVDAVRHLIAIAREKHhssgsaPNLSFHHLDIArdELPGAGTFDVLVSMHTLYWH 160
Cdd:COG4106     5 VLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARL------PNVRFVVADLR--DLDPPEPFDLVVSNAALHWL 76

                          90       100
                  ....*....|....*....|..
gi 1125442093 161 PDPAALLAASRRALKPGGHAIF 182
Cdd:COG4106    77 PDHAALLARLAAALAPGGVLAV 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-249 3.68e-15

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 70.92  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  60 MIEEIIALVTRSIPVTANPRSVkiLDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHHssgsapnlsfHHLDIAR 139
Cdd:pfam13489   5 RERLLADLLLRLLPKLPSPGRV--LDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVR----------FDQFDEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093 140 DELPGAGTFDVLVSMHTLYWHPDPAALLAASRRALKPGGHAIFLTYNRPARVVQTFREAHragglgaavgalrwlvptav 219
Cdd:pfam13489  73 EAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWP-------------------- 132

                         170       180       190
                  ....*....|....*....|....*....|
gi 1125442093 220 FERFRDCDHRYMSEPEFHEALDQAGFDVLE 249
Cdd:pfam13489 133 YLRPRNGHISLFSARSLKRLLEEAGFEVVS 162
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 54-187 4.91e-13

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: 66.55  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  54 FGPYESM----IEEIIALVTRSIPvtANPRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREkhHSSGSAPN 129
Cdd:TIGR01983  19 FKPLHKMnplrLDYIRDRIRKNFK--NPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEENIEVAKL--HAKKDPLQ 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1125442093 130 LSFHHLDIARDELPGAGTFDVLVSMHTLYWHPDPAALLAASRRALKPGGHAIFLTYNR 187
Cdd:TIGR01983  95 IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
46-182 8.97e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 65.02  E-value: 8.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  46 TYDAVVTRFGPYES---MIEEIIALVtrsipvtANPRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHH 122
Cdd:COG4976    17 SYDAALVEDLGYEApalLAEELLARL-------PPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGV 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093 123 SSgsapnlSFHHLDIARDELPGaGTFDVLVSMHTLYWHPDPAALLAASRRALKPGGHAIF 182
Cdd:COG4976    90 YD------RLLVADLADLAEPD-GRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIF 142
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 78-226 2.09e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.55  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  78 PRSVKILDIACGIGNVGLRLARR-GYTVVAVDAVRHLIAIAREKHHSSGsAPNLSFHHLDIARDELPGAGTFDVLVSMHT 156
Cdd:COG0500    25 PKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADLAELDPLPAESFDLVVAFGV 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125442093 157 LYWHPDPAALLAASRRAL--KPGGHaIFLTYNRPARVVQTFREAH-RAGGLGAAVGALRWLVPTAVFERFRDC 226
Cdd:COG0500   104 LHHLPPEEREALLRELARalKPGGV-LLLSASDAAAALSLARLLLlATASLLELLLLLRLLALELYLRALLAA 175
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 72-163 1.48e-11

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 62.55  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  72 IPVTANPRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHHSSGSAPNLSFHHLDIArdelPGAGTFDVL 151
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLE----SLLGRFDTV 131

                          90
                  ....*....|..
gi 1125442093 152 VSMHTLYWHPDP 163
Cdd:PRK07580  132 VCLDVLIHYPQE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-182 1.91e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.22  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  84 LDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHHSSGsapnLSFHHLDIarDELP-GAGTFDVLVSMHTLYWHPD 162
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG----LTFVVGDA--EDLPfPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 1125442093 163 PAALLAASRRALKPGGHAIF 182
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 82-154 2.78e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.55  E-value: 2.78e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1125442093  82 KILDIACGIGNVGLRLARR-GYTVVAVDAVRHLIAIAREKHHSSGSAPNLSFHHLDIArdELPGAGTFDVLVSM 154
Cdd:COG2230    54 RVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYR--DLPADGQFDAIVSI 125
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 82-182 2.96e-08

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: 50.51  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  82 KILDIACGIGNVGLRLARR-GYTVVAVDAVRHLIAIAREKHHSSGsAPNLSFHHLDIARDELPGAGTFDVLVSMHTL-YW 159
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPEADESFDVIISDPPLhHL 79

                          90       100
                  ....*....|....*....|...
gi 1125442093 160 HPDPAALLAASRRALKPGGHAIF 182
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
 82-181 3.15e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.02  E-value: 3.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  82 KILDIACGIGNVGLRLARR---GYTVVAVDAVRHLIAIAREkhHSSGSAPNLSFHHLDIarDELP-GAGTFDVLVSMHTL 157
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDA--DGLPfPDGSFDAVRSDRVL 97

                          90       100
                  ....*....|....*....|....
gi 1125442093 158 YWHPDPAALLAASRRALKPGGHAI 181
Cdd:PRK08317   98 QHLEDPARALAEIARVLRPGGRVV 121
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 81-197 4.42e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 51.26  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  81 VKILDIACGIGNVGLRLARRGY---TVVAVDAVRHLIAIAREKHHSSGSApNLSFHHLDIarDELPGA---GTFDVLVSM 154
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFD-NVEFEQGDI--EELPELledDKFDVVISN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1125442093 155 HTLYWHPDPAALLAASRRALKPGGHAIFLTYNRPARVVQTFRE 197
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKE 124
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 82-154 6.33e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 49.00  E-value: 6.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125442093  82 KILDIACGIGNVGLRLARRGYT---VVAVDAVRHLIAIAREKHHSSGSAPNLSFHHLDIarDELPGA-GTFDvLVSM 154
Cdd:PRK00216   54 KVLDLACGTGDLAIALAKAVGKtgeVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDA--EALPFPdNSFD-AVTI 127
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 54-194 7.81e-07

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 49.35  E-value: 7.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  54 FGPYESMIEEIIALVTRSI-------PVTANP-RSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIARekHHSSG 125
Cdd:PLN02396   98 FKPLHQMNPTRLAFIRSTLcrhfskdPSSAKPfEGLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIAR--LHADM 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093 126 SAPNLSFHHLDIARDELPGAG-TFDVLVSMHTLYWHPDPAALLAASRRALKPGGHAIFLTYNRPARVVQT 194
Cdd:PLN02396  176 DPVTSTIEYLCTTAEKLADEGrKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVLSTINRTMRAYAS 245
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 82-152 9.85e-07

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 49.02  E-value: 9.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125442093  82 KILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIARE--KHHssgSAPNLSFHHLDIARD--ELPGAGTFDVLV 152
Cdd:COG2265   236 RVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDAREnaRLN---GLKNVEFVAGDLEEVlpELLWGGRPDVVV 307
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 84-179 2.05e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.35  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  84 LDIACGIGNVGLRLAR--RGYTVVAVDAVRHLIAIAREKHHSSG--SAPNLSFHHLDIARDELPgagTFDVLVSMHTLYW 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERLAALGllNAVRVELFQLDLGELDPG---SFDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|
gi 1125442093 160 HPDPAALLAASRRALKPGGH 179
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGV 97
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
82-140 7.17e-05

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 43.61  E-value: 7.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1125442093  82 KILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHHSSGSApNLSFHHLDIARD 140
Cdd:PRK13168  300 RVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARRNGLD-NVTFYHANLEED 357
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 82-200 1.15e-04

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: 42.27  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  82 KILDIACGIGNVGLRLARRGYTV--VAVDavrhlIAIAREKHHSSGSAPNLSFHHLDIARDELPGaGTFDVLVSMHTLYW 159
Cdd:TIGR02072  37 SVLDIGCGTGYLTRALLKRFPQAefIALD-----ISAGMLAQAKTKLSENVQFICGDAEKLPLED-SSFDLIVSNLALQW 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1125442093 160 HPDPAALLAASRRALKPGGHAIFLTYnrparVVQTFREAHR 200
Cdd:TIGR02072 111 CDDLSQALSELARVLKPGGLLAFSTF-----GPGTLHELRQ 146
rADc smart00650
Ribosomal RNA adenine dimethylases;
68-153 1.87e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 40.96  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093   68 VTRSIPVTANPR-SVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKhhsSGSAPNLSFHHLDIARDELPgAG 146
Cdd:smart00650   1 VIDKIVRAANLRpGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREK---FAAADNLTVIHGDALKFDLP-KL 76


                   ....*..
gi 1125442093  147 TFDVLVS 153
Cdd:smart00650  77 QPYKVVG 83
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
61-186 2.38e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 41.49  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  61 IEEIIAlvtrsipvTANPRSVKILDIACGIGNVGLRLARRGYTVVAVDAVRHLIAIAREKHHSSGSAPNLSF-------- 132
Cdd:PRK11036   34 LDRLLA--------ELPPRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFihcaaqdi 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1125442093 133 -HHLDIARDelpgagtfdvLVSMH-TLYWHPDPAALLAASRRALKPGGHAIFLTYN 186
Cdd:PRK11036  106 aQHLETPVD----------LILFHaVLEWVADPKSVLQTLWSVLRPGGALSLMFYN 151
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 82-153 8.44e-04

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: 39.74  E-value: 8.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125442093  82 KILDIACGIGNVGLRLARRGY--TVVAVDAVRHLIAIAREKHHSSGSAPNLSFHHLDIAR-DELPGAGTFDVLVS 153
Cdd:COG4123    40 RVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEfAAELPPGSFDLVVS 114
PLN02244 PLN02244
tocopherol O-methyltransferase
 60-185 7.75e-03

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 37.03  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125442093  60 MIEEiiALVTRSIPVTANPRSVKILDIACGIGNVGLRLAR------RGYTVVAVDAVRHlIAIAREKhhssGSAPNLSFH 133
Cdd:PLN02244  101 MIEE--SLAWAGVPDDDEKRPKRIVDVGCGIGGSSRYLARkyganvKGITLSPVQAARA-NALAAAQ----GLSDKVSFQ 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1125442093 134 HLDiARDELPGAGTFDVLVSMHTLYWHPDPAALLAASRRALKPGGHAIFLTY 185
Cdd:PLN02244  174 VAD-ALNQPFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVTW 224
 
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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