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Conserved domains on  [gi|510143456|gb|AGN37187|]
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putative methyltransferase [Bacillus paralicheniformis ATCC 9945a]

Protein Classification

class I SAM-dependent DNA methyltransferase( domain architecture ID 11471966)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047
PubMed:  23180741|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
2-144 9.95e-36

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


:

Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 125.11  E-value: 9.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   2 IYKGFSGIYD-KLMSHAPYDEWVSWIEKTIGAQQKERI-RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAa 79
Cdd:COG4976   10 LFDQYADSYDaALVEDLGYEAPALLAEELLARLPPGPFgRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKG- 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510143456  80 vrqLDIQFFQQDMRELAGHGQEFDAVViCCDSLNYLkseKDVFNTFKNVFSLLKEGGLLLFDVHS 144
Cdd:COG4976   89 ---VYDRLLVADLADLAEPDGRFDLIV-AADVLTYL---GDLAAVFAGVARALKPGGLFIFSVED 146
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
2-144 9.95e-36

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 125.11  E-value: 9.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   2 IYKGFSGIYD-KLMSHAPYDEWVSWIEKTIGAQQKERI-RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAa 79
Cdd:COG4976   10 LFDQYADSYDaALVEDLGYEAPALLAEELLARLPPGPFgRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKG- 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510143456  80 vrqLDIQFFQQDMRELAGHGQEFDAVViCCDSLNYLkseKDVFNTFKNVFSLLKEGGLLLFDVHS 144
Cdd:COG4976   89 ---VYDRLLVADLADLAEPDGRFDLIV-AADVLTYL---GDLAAVFAGVARALKPGGLFIFSVED 146
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-136 4.68e-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: 4.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   40 ILDLACGTGEISVRLAEK-GYDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRELAGHGQEFDAVViCCDSLNYLkSE 118
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVV-SSGVLHHL-PD 78

                          90
                  ....*....|....*...
gi 510143456  119 KDVFNTFKNVFSLLKEGG 136
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-142 1.99e-17

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: 75.16  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  39 RILDLACGTGEISVRLAE-KGYDVTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRELA-GHGQEFDaVVICCDSLNYL 115
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPpEADESFD-VIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*..
gi 510143456 116 ksEKDVFNTFKNVFSLLKEGGLLLFDV 142
Cdd:cd02440   80 --VEDLARFLEEARRLLKPGGVLVLTL 104
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 20-112 3.36e-15

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 72.18  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  20 DEWVSWIEKTigAQQKERiRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQLD--IQFFQQDMRELAG 97
Cdd:PRK07580  50 DTVLSWLPAD--GDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDLESLLG 126

                         90
                 ....*....|....*
gi 510143456  98 hgqEFDAVViCCDSL 112
Cdd:PRK07580 127 ---RFDTVV-CLDVL 137
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 39-155 9.40e-15

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 70.98  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   39 RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQ--YKAAVRQLDIQFFQQDMRELAGhgqEFDAVViCCDSLNYLk 116
Cdd:TIGR02021  58 RVLDAGCGTGLLSIELAKRGAIVKAVDISEQMVQMARnrAQGRDVAGNVEFEVNDLLSLCG---EFDIVV-CMDVLIHY- 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 510143456  117 SEKDVFNTFKNVFSLLKEGGLLLFDVHSIY-----KMDVVFPGS 155
Cdd:TIGR02021 133 PASDMAKALGHLASLTKERVIFTFAPKTAWlaflkMIGELFPGS 176
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
39-139 1.05e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456    39 RILDLACGTGEISVRLAEK--GYDVTGIDISEDMLAQAQYKAAVRQLD--IQFFQQDMRELAGHGqeFDAVVICCDSLNY 114
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERhpHLQLHGYTISPEQAEVGRERIRALGLQgrIRIFYRDSAKDPFPD--TYDLVFGFEVIHH 79

                           90       100
                   ....*....|....*....|....*
gi 510143456   115 LKSEKDVfntFKNVFSLLKEGGLLL 139
Cdd:smart00828  80 IKDKMDL---FSNISRHLKDGGHLV 101
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
2-144 9.95e-36

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 125.11  E-value: 9.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   2 IYKGFSGIYD-KLMSHAPYDEWVSWIEKTIGAQQKERI-RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAa 79
Cdd:COG4976   10 LFDQYADSYDaALVEDLGYEAPALLAEELLARLPPGPFgRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKG- 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510143456  80 vrqLDIQFFQQDMRELAGHGQEFDAVViCCDSLNYLkseKDVFNTFKNVFSLLKEGGLLLFDVHS 144
Cdd:COG4976   89 ---VYDRLLVADLADLAEPDGRFDLIV-AADVLTYL---GDLAAVFAGVARALKPGGLFIFSVED 146
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 14-142 6.59e-34

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: 118.97  E-value: 6.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  14 MSH-APYDEWVSWIEKTIGAQQKERIRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAvrQLDIQFFQQDM 92
Cdd:COG2227    1 MSDpDARDFWDRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA--ELNVDFVQGDL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 510143456  93 RELAGHGQEFDaVVICCDSLNYLkseKDVFNTFKNVFSLLKEGGLLLFDV 142
Cdd:COG2227   79 EDLPLEDGSFD-LVICSEVLEHL---PDPAALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-136 4.68e-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: 4.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   40 ILDLACGTGEISVRLAEK-GYDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRELAGHGQEFDAVViCCDSLNYLkSE 118
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVV-SSGVLHHL-PD 78

                          90
                  ....*....|....*...
gi 510143456  119 KDVFNTFKNVFSLLKEGG 136
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 19-144 4.65e-27

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: 101.61  E-value: 4.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  19 YDEWVSWIEKtigAQQKERIRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRELAGH 98
Cdd:COG2226    8 YDGREALLAA---LGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFP 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 510143456  99 GQEFDAvVICCDSLNYLkseKDVFNTFKNVFSLLKEGGLLLFDVHS 144
Cdd:COG2226   85 DGSFDL-VISSFVLHHL---PDPERALAEIARVLKPGGRLVVVDFS 126
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 39-140 8.11e-23

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 91.14  E-value: 8.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  39 RILDLACGTGEISVRLAEK-GYDVTGIDISEDMLAQAQYKAAVRQLD--IQFFQQDMRELAGHGQeFDAVViCCDSLNYL 115
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLAdrVEVRLADYRDLPADGQ-FDAIV-SIGMFEHV 131

                         90       100
                 ....*....|....*....|....*
gi 510143456 116 kSEKDVFNTFKNVFSLLKEGGLLLF 140
Cdd:COG2230  132 -GPENYPAYFAKVARLLKPGGRLLL 155
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
39-142 3.16e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 87.57  E-value: 3.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  39 RILDLACGTGEISVRLAEK--GYDVTGIDISEDMLAQAQYKAAvrqlDIQFFQQDMRELAGHGQeFDAVViCCDSLNYLk 116
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLP----NVRFVVADLRDLDPPEP-FDLVV-SNAALHWL- 76

                         90       100
                 ....*....|....*....|....*.
gi 510143456 117 seKDVFNTFKNVFSLLKEGGLLLFDV 142
Cdd:COG4106   77 --PDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 35-145 3.16e-20

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 85.35  E-value: 3.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  35 KERIRILDLACGTGEISVRLAEK-GYDVTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRELAGHGQE-FDaVVICCDS 111
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELDPLPAEsFD-LVVAFGV 103

                         90       100       110
                 ....*....|....*....|....*....|....
gi 510143456 112 LNYLKSEKDVFnTFKNVFSLLKEGGLLLFDVHSI 145
Cdd:COG0500  104 LHHLPPEEREA-LLRELARALKPGGVLLLSASDA 136
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-142 1.99e-17

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: 75.16  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  39 RILDLACGTGEISVRLAE-KGYDVTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRELA-GHGQEFDaVVICCDSLNYL 115
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPpEADESFD-VIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*..
gi 510143456 116 ksEKDVFNTFKNVFSLLKEGGLLLFDV 142
Cdd:cd02440   80 --VEDLARFLEEARRLLKPGGVLVLTL 104
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-140 5.92e-17

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 73.47  E-value: 5.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   41 LDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAqyKAAVRQLDIQFFQQDMRELAGHGQEFDaVVICCDSLNYLkseKD 120
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELA--REKAPREGLTFVVGDAEDLPFPDNSFD-LVLSSEVLHHV---ED 74

                          90       100
                  ....*....|....*....|
gi 510143456  121 VFNTFKNVFSLLKEGGLLLF 140
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 20-112 3.36e-15

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 72.18  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  20 DEWVSWIEKTigAQQKERiRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQLD--IQFFQQDMRELAG 97
Cdd:PRK07580  50 DTVLSWLPAD--GDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDLESLLG 126

                         90
                 ....*....|....*
gi 510143456  98 hgqEFDAVViCCDSL 112
Cdd:PRK07580 127 ---RFDTVV-CLDVL 137
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-138 7.42e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 68.16  E-value: 7.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   41 LDLACGTGEISVRLAEK--GYDVTGIDISEDMLAQAQYKAAVRQLD----IQFFQQDMRELAGHGqeFDaVVICCDSLNY 114
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLnavrVELFQLDLGELDPGS--FD-VVVASNVLHH 77

                          90       100
                  ....*....|....*....|....
gi 510143456  115 LkseKDVFNTFKNVFSLLKEGGLL 138
Cdd:pfam08242  78 L---ADPRAVLRNIRRLLKPGGVL 98
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 39-155 9.40e-15

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 70.98  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   39 RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQ--YKAAVRQLDIQFFQQDMRELAGhgqEFDAVViCCDSLNYLk 116
Cdd:TIGR02021  58 RVLDAGCGTGLLSIELAKRGAIVKAVDISEQMVQMARnrAQGRDVAGNVEFEVNDLLSLCG---EFDIVV-CMDVLIHY- 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 510143456  117 SEKDVFNTFKNVFSLLKEGGLLLFDVHSIY-----KMDVVFPGS 155
Cdd:TIGR02021 133 PASDMAKALGHLASLTKERVIFTFAPKTAWlaflkMIGELFPGS 176
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 38-139 1.05e-14

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 69.37  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   38 IRILDLACGTGEISVRLAEKGY---DVTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRELAGH--GQEFDaVVICCDS 111
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPELleDDKFD-VVISNCV 83

                          90       100
                  ....*....|....*....|....*...
gi 510143456  112 LNYLKSEKDVFNtfkNVFSLLKEGGLLL 139
Cdd:pfam13847  84 LNHIPDPDKVLQ---EILRVLKPGGRLI 108
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 6-107 2.62e-13

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 67.10  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   6 FSGI---YDK---LMS---HapydewVSWIEKTIG-AQQKERIRILDLACGTGEISVRLAEKGYD---VTGIDISEDMLA 72
Cdd:PRK00216  17 FDSIapkYDLmndLLSfglH------RVWRRKTIKwLGVRPGDKVLDLACGTGDLAIALAKAVGKtgeVVGLDFSEGMLA 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 510143456  73 QAQYKAAVRQLD--IQFFQQDMRELAGHGQEFDAVVI 107
Cdd:PRK00216  91 VGREKLRDLGLSgnVEFVQGDAEALPFPDNSFDAVTI 127
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 30-143 3.76e-13

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 65.14  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   30 IGAQQKERIRILDLACGTGEISVRLAEKGYDVTGIDISEDMlaqaQYKAAVRQLDIQFFQQDMRELAGHgqeFDaVVICC 109
Cdd:pfam13489  16 LLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA----IERALLNVRFDQFDEQEAAVPAGK---FD-VIVAR 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 510143456  110 DSLNYLkseKDVFNTFKNVFSLLKEGGLLLFDVH 143
Cdd:pfam13489  88 EVLEHV---PDPPALLRQIAALLKPGGLLLLSTP 118
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 36-140 1.02e-10

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: 59.99  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   36 ERIRILDLACGTGEISVRLAEKGYDVTGI--DISEDMLAQAQYKAAVRqldIQFFQQDMRELAGHGQEFDaVVICCDSLN 113
Cdd:TIGR02072  34 IPASVLDIGCGTGYLTRALLKRFPQAEFIalDISAGMLAQAKTKLSEN---VQFICGDAEKLPLEDSSFD-LIVSNLALQ 109

                          90       100
                  ....*....|....*....|....*..
gi 510143456  114 YLKSEKDVfntFKNVFSLLKEGGLLLF 140
Cdd:TIGR02072 110 WCDDLSQA---LSELARVLKPGGLLAF 133
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 39-107 1.34e-10

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: 60.58  E-value: 1.34e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510143456  39 RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRELAGH---GQEFDAVVI 107
Cdd:COG2265  236 RVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKnVEFVAGDLEEVLPEllwGGRPDVVVL 308
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 39-106 1.03e-09

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: 57.08  E-value: 1.03e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510143456  39 RILDLACGTGEISVRLAEKGYD--VTGIDISEDMLAQAQYKAAVRQLD--IQFFQQDMRELAGHGQE--FDAVV 106
Cdd:COG4123   40 RVLDLGTGTGVIALMLAQRSPGarITGVEIQPEAAELARRNVALNGLEdrITVIHGDLKEFAAELPPgsFDLVV 113
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
10-139 3.55e-09

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 55.52  E-value: 3.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   10 YDK---LMSHAPYDEWVSWIEKTIGAqqKERIRILDLACGTGEISVRL---AEKGYDVTGIDISEDMLAQAQYKAA-VRQ 82
Cdd:pfam01209  15 YDLmndVISFGIHRLWKDFTMKCMGV--KRGNKFLDVAGGTGDWTFGLsdsAGSSGKVVGLDINENMLKEGEKKAKeEGK 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 510143456   83 LDIQFFQQDMRELAGHGQEFDAVVICCDslnyLKSEKDVFNTFKNVFSLLKEGGLLL 139
Cdd:pfam01209  93 YNIEFLQGNAEELPFEDDSFDIVTISFG----LRNFPDYLKVLKEAFRVLKPGGRVV 145
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 39-106 4.95e-08

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 52.64  E-value: 4.95e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510143456  39 RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRElAGHGQEFDAVV 106
Cdd:PRK12335 123 KALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINS-ASIQEEYDFIL 189
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 23-106 8.70e-08

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 51.70  E-value: 8.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  23 VSWIEKTIgaQQKERIRILDLACGTGEISVRLAE--KGYDVTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRElAGHG 99
Cdd:PRK09328  97 VEWALEAL--LLKEPLRVLDLGTGSGAIALALAKerPDAEVTAVDISPEALAVARRNAKHGLGArVEFLQGDWFE-PLPG 173


                 ....*..
gi 510143456 100 QEFDAVV 106
Cdd:PRK09328 174 GRFDLIV 180
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
38-138 1.83e-07

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 50.73  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  38 IRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQL--DIQFFQQDMRELAGHGQE------FDAVvicc 109
Cdd:PRK11036  46 LRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVsdNMQFIHCAAQDIAQHLETpvdlilFHAV---- 121

                         90       100
                 ....*....|....*....|....*....
gi 510143456 110 dsLNYLKSEKDVFNTfknVFSLLKEGGLL 138
Cdd:PRK11036 122 --LEWVADPKSVLQT---LWSVLRPGGAL 145
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 32-107 2.32e-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: 49.18  E-value: 2.32e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510143456  32 AQQKERIRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYK-AAVRQLDIQFFQQDMRELAGHGQEFDAVVI 107
Cdd:COG1041   22 AGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENlEHYGYEDADVIRGDARDLPLADESVDAIVT 98
PRK08317 PRK08317
hypothetical protein; Provisional
 39-108 2.37e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 50.32  E-value: 2.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510143456  39 RILDLACGTG----EISVRLAEKGyDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRELAGHGQEFDAVVIC 108
Cdd:PRK08317  22 RVLDVGCGPGndarELARRVGPEG-RVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAVRSD 94
PRK06202 PRK06202
hypothetical protein; Provisional
 33-108 2.90e-07

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 50.00  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  33 QQKERIRILDLACGTGEISVRLA----EKGYD--VTGIDISEDMLAQAQYKAAVRQLDIQFFQQDmrELAGHGQEFDaVV 106
Cdd:PRK06202  57 SADRPLTLLDIGCGGGDLAIDLArwarRDGLRleVTAIDPDPRAVAFARANPRRPGVTFRQAVSD--ELVAEGERFD-VV 133


                 ..
gi 510143456 107 IC 108
Cdd:PRK06202 134 TS 135
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 32-106 4.59e-07

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 49.76  E-value: 4.59e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510143456  32 AQQKERIRILDLACGTGEISVRLAE--KGYDVTGIDISEDMLAQAQYKAAVRQLD--IQFFQQDMRELAGHGQEFDAVV 106
Cdd:COG2890  108 LPAGAPPRVLDLGTGSGAIALALAKerPDARVTAVDISPDALAVARRNAERLGLEdrVRFLQGDLFEPLPGDGRFDLIV 186
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
25-140 1.10e-06

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 48.79  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  25 WIEKTIgaqQKERIRILDLACGTGEISVRLAE---KGYDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQD-MRELagHGQ 100
Cdd:COG0827  107 LVEKFT---KKEGLRILDPAVGTGNLLTTVLNqlkKKVNAYGVEVDDLLIRLAAVLANLQGHPVELFHQDaLQPL--LID 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 510143456 101 EFDAVVicCD-----------SLNY-LKSEKDVFNT----FKNVFSLLKEGGLLLF 140
Cdd:COG0827  182 PVDVVI--SDlpvgyypnderAKRFkLKADEGHSYAhhlfIEQSLNYLKPGGYLFF 235
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
39-106 1.96e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.21  E-value: 1.96e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510143456  39 RILDLACGTGEISVRLAEKG-YDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRELAGHGqEFDAVV 106
Cdd:COG2263   48 TVLDLGCGTGMLAIGAALLGaKKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPLGG-SVDTVV 115
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 26-112 4.13e-06

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 46.77  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  26 IEKTIGAQQKER----IRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQA--QYKAAVRQLDI----QFFQQDMREL 95
Cdd:PLN02585 130 VEKVLLWLAEDGslagVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAerRAKEALAALPPevlpKFEANDLESL 209

                         90
                 ....*....|....*..
gi 510143456  96 AGhgqEFDaVVICCDSL 112
Cdd:PLN02585 210 SG---KYD-TVTCLDVL 222
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 39-134 8.72e-06

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: 44.89  E-value: 8.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   39 RILDLACGTGEISVRLAEKGYD--VTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRELAGHGQeFDAVV--------- 106
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDaeLTMVDINARALESARENLAANGLEnGEVVASDVYSGVEDGK-FDLIIsnppfhagl 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 510143456  107 ---------ICCDSLNYLKSEKD---VFNTFKNVFSLLKE 134
Cdd:pfam05175 113 attynvaqrFIADAKRHLRPGGElwiVANRFLGYPPLLEE 152
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 40-79 1.20e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 45.13  E-value: 1.20e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 510143456  40 ILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAA 79
Cdd:PRK10258  46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDA 85
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 39-106 2.11e-05

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 44.03  E-value: 2.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510143456  39 RILDLACGTGEISVRLAEKGYD--VTGIDISEDMLAQAQYKAAVRQLD-IQFFQQDMRELAGHGQeFDAVV 106
Cdd:COG2813   52 RVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVELARANAAANGLEnVEVLWSDGLSGVPDGS-FDLIL 121
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 39-150 2.27e-05

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: 44.63  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   39 RILDLACGTGEISVRLAEKgYD--VTGIDISEDMLAQAQYKAAVRQL--DIQFFQQDMRELAGhgqEFDAVViccdSL-- 112
Cdd:pfam02353  64 TLLDIGCGWGGLMRRAAER-YDvnVVGLTLSKNQYKLARKRVAAEGLarKVEVLLQDYRDFDE---PFDRIV----SVgm 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 510143456  113 -------NYlksekDVFntFKNVFSLLKEGGLLLfdVHSIYKMDV 150
Cdd:pfam02353 136 fehvgheNY-----DTF--FKKLYNLLPPGGLML--LHTITGLHP 171
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
32-139 2.49e-05

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 44.38  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  32 AQQKERIRILDLACGTGE----ISVRLAEKG-------YDVTGIDISEDMLAQAQ---YKA-AVRQLD------------ 84
Cdd:COG1352   98 RRAGRPLRIWSAGCSTGEepysLAMLLAEAGgelagwrVEILATDISEEALEKARagiYPErSLRGLPpeylsryftkeg 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510143456  85 ------------IQFFQQDMRELAGHGQEFDaVVICCDSLNYLKSE--KDVFNTFKNvfsLLKEGGLLL 139
Cdd:COG1352  178 gryrikpelremVTFAQHNLLDDPPPFGRFD-LIFCRNVLIYFDPElqRRVLRRFHD---SLAPGGYLF 242
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 39-94 3.78e-05

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 42.92  E-value: 3.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 510143456   39 RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRE 94
Cdd:TIGR00537  22 DVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGLDVVMTDLFK 77
PRK14967 PRK14967
putative methyltransferase; Provisional
 39-106 8.87e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 42.35  E-value: 8.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510143456  39 RILDLACGTGEISVRLAEKG-YDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRElAGHGQEFDAVV 106
Cdd:PRK14967  39 RVLDLCTGSGALAVAAAAAGaGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWAR-AVEFRPFDVVV 106
PRK14968 PRK14968
putative methyltransferase; Provisional
 32-106 1.47e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 1.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510143456  32 AQQKERIRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAA---VRQLDIQFFQQDMRELAGhGQEFDAVV 106
Cdd:PRK14968  19 AVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKlnnIRNNGVEVIRSDLFEPFR-GDKFDVIL 95
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 32-106 1.72e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 42.03  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  32 AQQKERIRILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAavrQLD-----IQFFQQDMRELAGHGQEFDAVV 106
Cdd:PLN02396 127 AKPFEGLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHA---DMDpvtstIEYLCTTAEKLADEGRKFDAVL 203
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 39-138 1.97e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 41.47  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  39 RILDLACGTGEISVRLAEK--GYDVTGIDISEDMLAQAQykaaVRQLDIQFFQQDMRELAGhGQEFDaVVICCDSLNYLK 116
Cdd:PRK01683  34 YVVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEAR----SRLPDCQFVEADIASWQP-PQALD-LIFANASLQWLP 107

                         90       100
                 ....*....|....*....|..
gi 510143456 117 SEKDVfntFKNVFSLLKEGGLL 138
Cdd:PRK01683 108 DHLEL---FPRLVSLLAPGGVL 126
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 26-139 4.42e-04

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 39.96  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   26 IEKTIGAQQKERIRILDLACGTGE----ISVRLAEK-------GYDVTGIDISEDMLAQAQ---YKA-AVRQLDIQFFQQ 90
Cdd:pfam01739  20 LPLLAKAKNGKRVRIWSAGCSSGEepysLAMLLKETfpnaarwDFKILATDIDLSVLEKARagvYPErELEGLPEELLRR 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510143456   91 DMRELAGHGQEFDAVV---ICCDSLNyLKSEKDVFNTF-----KNVF----------------SLLKEGGLLL 139
Cdd:pfam01739 100 YFEKTAGGGYTVKPEIksmVLFEYLN-LLDEYPPLGDFdvifcRNVLiyfdeetqrkilnrfaEKLKPGGYLF 171
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
39-139 1.05e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456    39 RILDLACGTGEISVRLAEK--GYDVTGIDISEDMLAQAQYKAAVRQLD--IQFFQQDMRELAGHGqeFDAVVICCDSLNY 114
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERhpHLQLHGYTISPEQAEVGRERIRALGLQgrIRIFYRDSAKDPFPD--TYDLVFGFEVIHH 79

                           90       100
                   ....*....|....*....|....*
gi 510143456   115 LKSEKDVfntFKNVFSLLKEGGLLL 139
Cdd:smart00828  80 IKDKMDL---FSNISRHLKDGGHLV 101
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
39-65 1.54e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 38.56  E-value: 1.54e-03
                         10        20
                 ....*....|....*....|....*..
gi 510143456  39 RILDLACGTGEISVRLAEKGYDVTGID 65
Cdd:PRK11207  33 KTLDLGCGNGRNSLYLAANGFDVTAWD 59
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 9-135 2.58e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 38.33  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   9 IYDKL---MSHAPYDEW----VSWIEKTIGAqqkeriRILDLACGTGEISVRLAEK-GYD--VTGIDISEDMLAQA---- 74
Cdd:PLN02233  45 VYDNLndlLSLGQHRIWkrmaVSWSGAKMGD------RVLDLCCGSGDLAFLLSEKvGSDgkVMGLDFSSEQLAVAasrq 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510143456  75 QYKAAVRQLDIQFFQQDMRELAGHGQEFDAVviccdSLNY-LKSEKDVFNTFKNVFSLLKEG 135
Cdd:PLN02233 119 ELKAKSCYKNIEWIEGDATDLPFDDCYFDAI-----TMGYgLRNVVDRLKAMQEMYRVLKPG 175
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 39-106 3.46e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 38.10  E-value: 3.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510143456   39 RILDLACGTGEISVRLAEKGYD--VTGIDISEDMLAQAQYKAAVRQL--DIQFFQQDMRE-LAghGQEFDAVV 106
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNaeVIAVDISPDALAVAEENAEKNQLehRVEFIQSNLFEpLA--GQKIDIIV 187
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 39-158 3.87e-03

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 37.77  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456   39 RILDLACGTGEISVRLAEKGYD-VTGIDISEDMLAQAQykaAVRQL--------DIQFFQQDMRELAGhgqeFDaVVICC 109
Cdd:pfam08003 118 TILDVGCGNGYHMWRMLGEGAAmVVGIDPSELFLCQFE---AVRKLlgndqrahLLPLGIEQLPALAA----FD-TVFSM 189

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 510143456  110 DSLNYLKSEKDVFNTFKNvfSLLKEGGLLL------FDVHsiykmDVVFPGSTYA 158
Cdd:pfam08003 190 GVLYHRRSPLDHLLQLKD--QLVKGGELVLetlvidGDEN-----TVLVPGDRYA 237
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 4-75 4.69e-03

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 37.65  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456     4 KGFSGIYDKLMSHAPYDEWVSWIEK-TIG-------------------------AQQKERIRILDLACGTGE----ISVR 53
Cdd:smart00138  41 KDFSEYLELLTSHRGEEELAELLDLmTTNetrffreskhfealeekvlplliasRRHGRRVRIWSAGCSTGEepysLAML 120

                           90       100
                   ....*....|....*....|....*....
gi 510143456    54 LAEKG-------YDVTGIDISEDMLAQAQ 75
Cdd:smart00138 121 LAETLpkgrepdVKILATDIDLKALEKAR 149
TehB pfam03848
Tellurite resistance protein TehB;
39-84 6.68e-03

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 36.75  E-value: 6.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 510143456   39 RILDLACGTGEISVRLAEKGYDVTGIDISEDMLAQAQYKAAVRQLD 84
Cdd:pfam03848  33 KVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLD 78
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 39-139 9.30e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.04  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510143456  39 RILDLACGTGEISVRLAEK-GYDVTGIDISEDMLAQAQYKAAVRQLDIQFFQQDMRELAGHGQEFDaVVICCDSLNYLKS 117
Cdd:PLN02336 269 KVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFD-VIYSRDTILHIQD 347

                         90       100
                 ....*....|....*....|..
gi 510143456 118 EKDVFNTFknvFSLLKEGGLLL 139
Cdd:PLN02336 348 KPALFRSF---FKWLKPGGKVL 366
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 35-107 9.82e-03

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: 36.28  E-value: 9.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510143456   35 KERIRILDLACGTGEISVRLAE-KGYDVTGIDISEDMLAQAQYKAavrqldIQFFQQDMRELAGHGQE--FDAVVI 107
Cdd:pfam07021  12 PPGSRVLDLGCGDGTLLYLLKEeKGVDGYGIELDAAGVAECVAKG------LYVIQGDLDEGLEHFPDksFDYVIL 81
 
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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