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Conserved domains on  [gi|447014802|ref|WP_001092058|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacteria]

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]; ...
 8-134 1.06e-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: 110.08  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   8 FDKVAEDYDFVNELLNDysffvsnMSPKKG-RALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSK--RQLTNTVY 84
Cdd:COG2226    1 FDRVAARYDGREALLAA-------LGLRPGaRVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaEAGLNVEF 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447014802  85 LNMNAEQLNF-NEKFDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVILD 134
Cdd:COG2226   74 VVGDAEDLPFpDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 8-134 1.06e-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: 110.08  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   8 FDKVAEDYDFVNELLNDysffvsnMSPKKG-RALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSK--RQLTNTVY 84
Cdd:COG2226    1 FDRVAARYDGREALLAA-------LGLRPGaRVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaEAGLNVEF 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447014802  85 LNMNAEQLNF-NEKFDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVILD 134
Cdd:COG2226   74 VVGDAEDLPFpDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-132 1.49e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 90.03  E-value: 1.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   40 LDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQLTNTVYLNMNAEQLNFNEK-FDFIVSRTTFHHLDDIASVIQ 118
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNsFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 447014802  119 QMKELLNEEGRIVI 132
Cdd:pfam08241  81 EIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
 32-135 1.09e-18

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 81.14  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  32 MSPKKG-RALDIGCGSGLLVEKLASYYD---EVVGIDISNQMLDLAKSKR--QLTNTVYLNMNAEQLNF-NEKFDFIVSR 104
Cdd:PRK08317  15 LAVQPGdRVLDVGCGPGNDARELARRVGpegRVVGIDRSEAMLALAKERAagLGPNVEFVRGDADGLPFpDGSFDAVRSD 94

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447014802 105 TTFHHLDDIASVIQQMKELLNEEGRIVILDN 135
Cdd:PRK08317  95 RVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 38-132 1.30e-15

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 69.77  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  38 RALDIGCGSGLLVEKLASYYD-EVVGIDISNQMLDLAKSKRQL---TNTVYLNMNAEQLNF--NEKFDFIVSRTTFHHL- 110
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGaRVTGVDISPVALELARKAAAAllaDNVEVLKGDAEELPPeaDESFDVIISDPPLHHLv 80

                         90       100
                 ....*....|....*....|..
gi 447014802 111 DDIASVIQQMKELLNEEGRIVI 132
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVL 102
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 8-128 1.97e-14

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: 69.62  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802    8 FDKVAEDYDFVNEL-----LNDYSFFVSNMSPKKGRALDIGCGSGLLVEKLASYY--DEVVGIDISNQMLDLAKSKRQLT 80
Cdd:TIGR02072   2 FNKAAKTYDRHAKIqremaKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSEN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 447014802   81 NTvYLNMNAEQLNF-NEKFDFIVSRTTFHHLDDIASVIQQMKELLNEEG 128
Cdd:TIGR02072  82 VQ-FICGDAEKLPLeDSSFDLIVSNLALQWCDDLSQALSELARVLKPGG 129
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
38-142 5.08e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.01  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802    38 RALDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKSK---RQLTNTVYL-NMNAEQLNFNEKFDFIVSRTTFHHLD 111
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERiraLGLQGRIRIfYRDSAKDPFPDTYDLVFGFEVIHHIK 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 447014802   112 DIASVIQQMKELLNEEGRIVILDNVSEVETP 142
Cdd:smart00828  82 DKMDLFSNISRHLKDGGHLVLADFIANLLSA 112
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 8-134 1.06e-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: 110.08  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   8 FDKVAEDYDFVNELLNDysffvsnMSPKKG-RALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSK--RQLTNTVY 84
Cdd:COG2226    1 FDRVAARYDGREALLAA-------LGLRPGaRVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaEAGLNVEF 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447014802  85 LNMNAEQLNF-NEKFDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVILD 134
Cdd:COG2226   74 VVGDAEDLPFpDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-132 6.47e-28

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: 102.40  E-value: 6.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  28 FVSNMSPKKGRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQLTNTVYLNMNAEQLNF-NEKFDFIVSRTT 106
Cdd:COG2227   17 LLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLeDGSFDLVICSEV 96

                         90       100
                 ....*....|....*....|....*.
gi 447014802 107 FHHLDDIASVIQQMKELLNEEGRIVI 132
Cdd:COG2227   97 LEHLPDPAALLRELARLLKPGGLLLL 122
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
37-132 1.25e-25

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 95.66  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  37 GRALDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKskRQLTNTVYLNMNAEQLNFNEKFDFIVSRTTFHHLDDIA 114
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARAR--ARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHA 80

                         90
                 ....*....|....*...
gi 447014802 115 SVIQQMKELLNEEGRIVI 132
Cdd:COG4106   81 ALLARLAAALAPGGVLAV 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
2-132 1.67e-24

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 95.07  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   2 NTIESQFDKVAEDYDFVNELLNDY--------SFFVSNMSPKKGRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLA 73
Cdd:COG4976    5 AYVEALFDQYADSYDAALVEDLGYeapallaeELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 447014802  74 KSKRQLTNTVYLNMnAEQLNFNEKFDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVI 132
Cdd:COG4976   85 REKGVYDRLLVADL-ADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIF 142
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-132 1.49e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 90.03  E-value: 1.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   40 LDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQLTNTVYLNMNAEQLNFNEK-FDFIVSRTTFHHLDDIASVIQ 118
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNsFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 447014802  119 QMKELLNEEGRIVI 132
Cdd:pfam08241  81 EIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-128 6.10e-22

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 86.08  E-value: 6.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   40 LDIGCGSGLLVEKLASYYD-EVVGIDISNQMLDLAKSK--RQLTNTVYLNMNAEQLNF-NEKFDFIVSRTTFHHL--DDI 113
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERaaEAGLNVEFVQGDAEDLPFpDGSFDLVVSSGVLHHLpdPDL 81

                          90
                  ....*....|....*
gi 447014802  114 ASVIQQMKELLNEEG 128
Cdd:pfam13649  82 EAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 34-132 8.73e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 80.73  E-value: 8.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  34 PKKGRALDIGCGSGLLVEKLASYY-DEVVGIDISNQMLDLAK---SKRQLTNTVYLNMNAEQLNFN--EKFDFIVSRTTF 107
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARFgGRVIGIDLSPEAIALARaraAKAGLGNVEFLVADLAELDPLpaESFDLVVAFGVL 104

                         90       100
                 ....*....|....*....|....*..
gi 447014802 108 HHLD--DIASVIQQMKELLNEEGRIVI 132
Cdd:COG0500  105 HHLPpeEREALLRELARALKPGGVLLL 131
PRK08317 PRK08317
hypothetical protein; Provisional
 32-135 1.09e-18

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 81.14  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  32 MSPKKG-RALDIGCGSGLLVEKLASYYD---EVVGIDISNQMLDLAKSKR--QLTNTVYLNMNAEQLNF-NEKFDFIVSR 104
Cdd:PRK08317  15 LAVQPGdRVLDVGCGPGNDARELARRVGpegRVVGIDRSEAMLALAKERAagLGPNVEFVRGDADGLPFpDGSFDAVRSD 94

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447014802 105 TTFHHLDDIASVIQQMKELLNEEGRIVILDN 135
Cdd:PRK08317  95 RVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 38-132 1.16e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.20  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  38 RALDIGCGSGLLVEKLASYYD-EVVGIDISNQMLDLAKSK---RQLTNTV-YLNMNAEQLNFNEKFDFIVSRTTFHHL-- 110
Cdd:COG2230   54 RVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERaaeAGLADRVeVRLADYRDLPADGQFDAIVSIGMFEHVgp 133

                         90       100
                 ....*....|....*....|..
gi 447014802 111 DDIASVIQQMKELLNEEGRIVI 132
Cdd:COG2230  134 ENYPAYFAKVARLLKPGGRLLL 155
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-130 5.79e-18

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 75.87  E-value: 5.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   40 LDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKSK-RQLTNTVYLNMNAEQLNFNE----KFDFIVSRTTFHHLDD 112
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPglEYTGLDISPAALEAARERlAALGLLNAVRVELFQLDLGEldpgSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 447014802  113 IASVIQQMKELLNEEGRI 130
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 34-134 4.51e-17

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 75.16  E-value: 4.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   34 PKKGRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQltNTVYLNMNAEQLNfnEKFDFIVSRTTFHHLDDI 113
Cdd:pfam13489  21 PSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVR--FDQFDEQEAAVPA--GKFDVIVAREVLEHVPDP 96

                          90       100
                  ....*....|....*....|.
gi 447014802  114 ASVIQQMKELLNEEGRIVILD 134
Cdd:pfam13489  97 PALLRQIAALLKPGGLLLLST 117
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 38-132 1.30e-15

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 69.77  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  38 RALDIGCGSGLLVEKLASYYD-EVVGIDISNQMLDLAKSKRQL---TNTVYLNMNAEQLNF--NEKFDFIVSRTTFHHL- 110
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGaRVTGVDISPVALELARKAAAAllaDNVEVLKGDAEELPPeaDESFDVIISDPPLHHLv 80

                         90       100
                 ....*....|....*....|..
gi 447014802 111 DDIASVIQQMKELLNEEGRIVI 132
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVL 102
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 8-128 1.97e-14

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: 69.62  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802    8 FDKVAEDYDFVNEL-----LNDYSFFVSNMSPKKGRALDIGCGSGLLVEKLASYY--DEVVGIDISNQMLDLAKSKRQLT 80
Cdd:TIGR02072   2 FNKAAKTYDRHAKIqremaKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSEN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 447014802   81 NTvYLNMNAEQLNF-NEKFDFIVSRTTFHHLDDIASVIQQMKELLNEEG 128
Cdd:TIGR02072  82 VQ-FICGDAEKLPLeDSSFDLIVSNLALQWCDDLSQALSELARVLKPGG 129
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 35-143 2.01e-14

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 67.83  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   35 KKGRALDIGCGSGLLVEKLASYYD---EVVGIDISNQMLDLAKSKRQLTNtvYLNMNAEQLNFNE--------KFDFIVS 103
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLG--FDNVEFEQGDIEElpelleddKFDVVIS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 447014802  104 RTTFHHLDDIASVIQQMKELLNEEGRIVILDNVSEVETPP 143
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPA 120
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 4-149 8.09e-14

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 67.87  E-value: 8.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   4 IESQFDKVAEDYDFVNELLndySF---------FVSNMSPKKG-RALDIGCGSGLLVEKLASYYD---EVVGIDISNQML 70
Cdd:PRK00216  13 VAEMFDSIAPKYDLMNDLL---SFglhrvwrrkTIKWLGVRPGdKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGML 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  71 DLAKsKRQLTNTVYLNM-----NAEQLNF-NEKFDFI--------VSrttfhhldDIASVIQQMKELLNEEGRIVILDnV 136
Cdd:PRK00216  90 AVGR-EKLRDLGLSGNVefvqgDAEALPFpDNSFDAVtiafglrnVP--------DIDKALREMYRVLKPGGRLVILE-F 159

                        170
                 ....*....|....
gi 447014802 137 SEVETPPTY-VYKL 149
Cdd:PRK00216 160 SKPTNPPLKkAYDF 173
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 38-132 3.39e-10

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: 57.69  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   38 RALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQLTNTV--YLNMNAEQL--NFNEKFDFIVSRTTFHHLDDI 113
Cdd:TIGR01983  49 RVLDVGCGGGLLSEPLARLGANVTGIDASEENIEVAKLHAKKDPLQidYRCTTVEDLaeKKAGSFDVVTCMEVLEHVPDP 128

                          90
                  ....*....|....*....
gi 447014802  114 ASVIQQMKELLNEEGRIVI 132
Cdd:TIGR01983 129 QAFIRACAQLLKPGGILFF 147
ovoA_Cterm TIGR04345
putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. ...
 35-132 6.51e-10

putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 275141  Cd Length: 242  Bit Score: 57.23  E-value: 6.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   35 KKGRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLA---KSKRQLTNTV--------YLNMNAEQLNFNEK------ 97
Cdd:TIGR04345  41 SRKRALDIGCAVGRASFELARYFDEVDGIDFSARFIRPAvalKERGSLRYALkeegelvsFKEVTLSDLGLDEVrdrvsf 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 447014802   98 --------------FDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVI 132
Cdd:TIGR04345 121 fqgdacnlkphftgYDLILAANLLDRLYDPAAFLSSIHERLNPGGLLVI 169
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
8-143 4.41e-09

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 54.75  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802    8 FDKVAEDYDFVNELLND------YSFFVSNMSPKKG-RALDIGCGSGLLVEKLASYYD---EVVGIDISNQMLDLAKSKR 77
Cdd:pfam01209   8 FSSVASKYDLMNDVISFgihrlwKDFTMKCMGVKRGnKFLDVAGGTGDWTFGLSDSAGssgKVVGLDINENMLKEGEKKA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   78 Q---LTNTVYLNMNAEQLNF-NEKFDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVILDnVSEVETPP 143
Cdd:pfam01209  88 KeegKYNIEFLQGNAEELPFeDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLE-FSKPENPL 156
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 27-135 9.28e-08

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: 49.90  E-value: 9.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   27 FFVSNMS-PKKGRALDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKSKRQLTN----TVYLNMNAEQLnFNEKFD 99
Cdd:pfam05175  22 LLLEHLPkDLSGKVLDLGCGAGVLGAALAKESPdaELTMVDINARALESARENLAANGlengEVVASDVYSGV-EDGKFD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 447014802  100 FIVSRTTFH-HLDDIASVIQQM----KELLNEEGRIVILDN 135
Cdd:pfam05175 101 LIISNPPFHaGLATTYNVAQRFiadaKRHLRPGGELWIVAN 141
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 35-142 1.04e-07

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 51.10  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  35 KKGRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQLTNtvyLNMNA-----EQLNFNEKFDFIVSRTTFHH 109
Cdd:PRK12335 120 KPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKEN---LNIRTglydiNSASIQEEYDFILSTVVLMF 196

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447014802 110 L--DDIASVIQQMKELLNEEGRIVIldnVSEVETP 142
Cdd:PRK12335 197 LnrERIPAIIKNMQEHTNPGGYNLI---VCAMDTE 228
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 34-132 1.54e-07

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: 50.14  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  34 PKKGRALDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKSkrqltnTVYLNMNAEQLNF-------------NEKF 98
Cdd:COG4123   36 KKGGRVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARR------NVALNGLEDRITVihgdlkefaaelpPGSF 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447014802  99 DFIVS-----------------RTTFHHLD--DIASVIQQMKELLNEEGRIVI 132
Cdd:COG4123  110 DLVVSnppyfkagsgrkspdeaRAIARHEDalTLEDLIRAAARLLKPGGRFAL 162
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 34-132 3.26e-07

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 49.39  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   34 PKKGRALDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKSKRQltntvylNMNAEQLNF----------NEKFDFI 101
Cdd:TIGR03534  85 KKGPRVLDLGTGSGAIALALAKERPdaRVTAVDISPEALAVARKNAR-------RLGLENVEFlqgdwfeplpSGKFDLI 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 447014802  102 VS--------------RTTFHH------------LDDIASVIQQMKELLNEEGRIVI 132
Cdd:TIGR03534 158 VSnppyipeadihlldPEVRDFeprlalfggedgLDFYRRIIAQAPRLLKPGGWLLL 214
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 33-132 9.67e-07

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: 47.87  E-value: 9.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   33 SPKKGRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQlTNTVYLNMNAE---QLNFNEKFDFIVSRTTFHH 109
Cdd:TIGR02021  53 PLKGKRVLDAGCGTGLLSIELAKRGAIVKAVDISEQMVQMARNRAQ-GRDVAGNVEFEvndLLSLCGEFDIVVCMDVLIH 131

                          90       100
                  ....*....|....*....|....*
gi 447014802  110 --LDDIASVIQQMKELLNEegRIVI 132
Cdd:TIGR02021 132 ypASDMAKALGHLASLTKE--RVIF 154
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 38-205 3.22e-06

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: 46.55  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   38 RALDIGCGSGLLVEKLASYYD-EVVGIDIS-NQmldlAKSKRQLTNTVYLNMNAEQL-----NFNEKFDFIVSRTTFHHL 110
Cdd:pfam02353  64 TLLDIGCGWGGLMRRAAERYDvNVVGLTLSkNQ----YKLARKRVAAEGLARKVEVLlqdyrDFDEPFDRIVSVGMFEHV 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  111 --DDIASVIQQMKELLNEEGR-----IVILDN--VSEVETPPTYVYK----------LGAIQEFLPHC-FKFGIKNAIRI 170
Cdd:pfam02353 140 ghENYDTFFKKLYNLLPPGGLmllhtITGLHPdeTSERGLPLKFIDKyifpggelpsISMIVESSSEAgFTVEDVESLRP 219

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 447014802  171 YNHNTSKSWLEHLASDK----YLSEQNYYDLYEKLLPGC 205
Cdd:pfam02353 220 HYAKTLDLWAENLQANKdeaiALQSEEFYRMWMLYLTGC 258
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
38-134 5.29e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 45.91  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  38 RALDIGCGSGLL---VEKL-ASyydEVVGIDISNQMLDLAKSKRQLtNTVYLNMNAEQlnFNEKFDFIVSRTtfhhlddI 113
Cdd:PRK00517 122 TVLDVGCGSGILaiaAAKLgAK---KVLAVDIDPQAVEAARENAEL-NGVELNVYLPQ--GDLKADVIVANI-------L 188

                         90       100
                 ....*....|....*....|....*...
gi 447014802 114 ASVI----QQMKELLNEEGRIV---ILD 134
Cdd:PRK00517 189 ANPLlelaPDLARLLKPGGRLIlsgILE 216
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 34-132 5.39e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.92  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  34 PKKGRALDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKSkrqltNTVYLnmNAEQLNF----------NEKFDFI 101
Cdd:PRK09328 107 KEPLRVLDLGTGSGAIALALAKERPdaEVTAVDISPEALAVARR-----NAKHG--LGARVEFlqgdwfeplpGGRFDLI 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447014802 102 VS------RTTFHH--------------------LDDIASVIQQMKELLNEEGRIVI 132
Cdd:PRK09328 180 VSnppyipEADIHLlqpevrdhephlalfggedgLDFYRRIIEQAPRYLKPGGWLLL 236
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 34-132 5.67e-06

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: 45.18  E-value: 5.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  34 PKKGRALDIGCGSGLLVEKLASYYDE--VVGIDISNQMLDLAK---SKRQLTN-TVYLNMNAEQLNfNEKFDFIVS---- 103
Cdd:COG2813   48 PLGGRVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVELARanaAANGLENvEVLWSDGLSGVP-DGSFDLILSnppf 126

                         90       100       110
                 ....*....|....*....|....*....|
gi 447014802 104 RTTFHHLDDIA-SVIQQMKELLNEEGRIVI 132
Cdd:COG2813  127 HAGRAVDKEVAhALIADAARHLRPGGELWL 156
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 30-132 6.99e-06

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 45.88  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  30 SNMSPKKG-RALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAKSKRQL---TNTV-YLNMNAEQL-NFNEKFDFIVS 103
Cdd:PLN02396 125 SSAKPFEGlKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMdpvTSTIeYLCTTAEKLaDEGRKFDAVLS 204

                         90       100
                 ....*....|....*....|....*....
gi 447014802 104 RTTFHHLDDIASVIQQMKELLNEEGRIVI 132
Cdd:PLN02396 205 LEVIEHVANPAEFCKSLSALTIPNGATVL 233
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 28-142 1.56e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.13  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  28 FVSNMSPKKG-RALDIGCGSGLLVEKLASYYD-EVVGIDISNQMLDLAkskrqLTNTVYLNMNAE-------QLNF-NEK 97
Cdd:PLN02336 258 FVDKLDLKPGqKVLDVGCGIGGGDFYMAENFDvHVVGIDLSVNMISFA-----LERAIGRKCSVEfevadctKKTYpDNS 332

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447014802  98 FDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVILDNVSEVETP 142
Cdd:PLN02336 333 FDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTP 377
TehB pfam03848
Tellurite resistance protein TehB;
35-144 3.29e-05

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 43.30  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   35 KKGRALDIGCGSGLlveklASYYDEVVGIDIS----NQM----LDLAKSKRQLTNTVYLNMNAEQLNFNEKFDFIVSRTT 106
Cdd:pfam03848  30 KPGKVLDLGCGQGR-----NSLYLSLLGYDVTawdkNENsianLQRIKEKENLDNIHTALYDINNATIDENYDFILSTVV 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 447014802  107 FHHLDD--IASVIQQMKELLNEEGRIVILDNVSEVETPPT 144
Cdd:pfam03848 105 LMFLEPerIPGIIANMQECTNPGGYNLIVAAMSTDDVPCT 144
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
34-131 3.95e-05

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 43.77  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  34 PKKGRALDIGCGSGLLVEKLASYYDEV--VGIDISnqMLDLAKSKR-----QLTNTVYlnmnAEQL--NFNEKFDFIVSR 104
Cdd:PRK09489 195 HTKGKVLDVGCGAGVLSAVLARHSPKIrlTLSDVS--AAALESSRAtlaanGLEGEVF----ASNVfsDIKGRFDMIISN 268

                         90       100       110
                 ....*....|....*....|....*....|....
gi 447014802 105 TTFH-----HLDDIASVIQQMKELLNEEG--RIV 131
Cdd:PRK09489 269 PPFHdgiqtSLDAAQTLIRGAVRHLNSGGelRIV 302
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
38-136 4.08e-05

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 43.71  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  38 RALDIGCGSGLLVEKLASYYDE--VVGIDISNQMLDLAKSKRQLTNTVYLNMNAEQLNFNEKF-----DFIVSRTTFHHL 110
Cdd:PRK06922 421 TIVDVGAGGGVMLDMIEEETEDkrIYGIDISENVIDTLKKKKQNEGRSWNVIKGDAINLSSSFekesvDTIVYSSILHEL 500

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447014802 111 -------------DDIASVIQQMKELLNEEGRIVILDNV 136
Cdd:PRK06922 501 fsyieyegkkfnhEVIKKGLQSAYEVLKPGGRIIIRDGI 539
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 34-74 4.43e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 42.90  E-value: 4.43e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 447014802  34 PKKGRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAK 74
Cdd:PRK07580  62 LTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEAR 102
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
32-132 4.63e-05

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 43.31  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  32 MSPKKGR-ALDIGCGSGllveklasYY---------DEVVGIDISN----QMLDLAKSKRQLTNTVYLNMNAEQLNFNEK 97
Cdd:PRK15068 118 LSPLKGRtVLDVGCGNG--------YHmwrmlgagaKLVVGIDPSQlflcQFEAVRKLLGNDQRAHLLPLGIEQLPALKA 189

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447014802  98 FDFIVSRTTFHHLDDIASVIQQMKELLNEEGRIVI 132
Cdd:PRK15068 190 FDTVFSMGVLYHRRSPLDHLKQLKDQLVPGGELVL 224
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 33-132 4.81e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.21  E-value: 4.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  33 SPKKGRALDIGCGSG--LLVekLASYYD--EVVGIDISNQMLDLAKS---KRQLTNTVYL---NMnAEQLNFNEKFDFIV 102
Cdd:COG2890  110 AGAPPRVLDLGTGSGaiALA--LAKERPdaRVTAVDISPDALAVARRnaeRLGLEDRVRFlqgDL-FEPLPGDGRFDLIV 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447014802 103 S-----RTTFHH---------------------LDDIASVIQQMKELLNEEGRIVI 132
Cdd:COG2890  187 SnppyiPEDEIAllppevrdheprlaldggedgLDFYRRIIAQAPRLLKPGGWLLL 242
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 40-132 9.61e-05

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 42.25  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   40 LDIGCGSGLLveKLASYY---DEVVGIDISNQMLDLAKSKRQLtNTVYLNMNAEQLN--FNEKFDFIVSRTTFHHLDDIA 114
Cdd:pfam06325 166 LDVGCGSGIL--AIAALKlgaKKVVGVDIDPVAVRAAKENAEL-NGVEARLEVYLPGdlPKEKADVVVANILADPLIELA 242

                          90
                  ....*....|....*...
gi 447014802  115 sviQQMKELLNEEGRIVI 132
Cdd:pfam06325 243 ---PDIYALVKPGGYLIL 257
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
38-109 1.69e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 41.76  E-value: 1.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447014802  38 RALDIGCGSGLLVEKLASYYD-EVVGIDISNQMLDLAKSKRQ-LTNTVYLnMNAEQLnfNEKFDFIVSRTTFHH 109
Cdd:PRK11705 170 RVLDIGCGWGGLARYAAEHYGvSVVGVTISAEQQKLAQERCAgLPVEIRL-QDYRDL--NGQFDRIVSVGMFEH 240
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 32-155 2.14e-04

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 40.90  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  32 MSPKKGRALDIGCGSGL--LVekLASYYDE--VVGIDiSNQM----LDLAKSKRQLTNTVYLNMNAEQLNFNEKFDFIVS 103
Cdd:COG0357   64 LPKEGARVLDVGSGAGFpgIP--LAIARPDlqVTLVD-SLGKkiafLREVVRELGLKNVTVVHGRAEELAPREKFDVVTA 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447014802 104 RtTFHHLDDIASVIqqmKELLNEEGRIVIL---DNVSEVETPPTYVYKLGAIQEF 155
Cdd:COG0357  141 R-AVAPLPDLLELA---LPLLKPGGRLLALkgpDAEEELAEAPKALKVLEEVEEL 191
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
38-117 4.41e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 39.89  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  38 RALDIGCGSGLLVekLASYY---DEVVGIDISNQMLDLAKS--KRQLTNTVYLNMNAEQLNFNEKFDFIVSRTTF----H 108
Cdd:COG2263   48 TVLDLGCGTGMLA--IGAALlgaKKVVGVDIDPEALEIAREnaERLGVRVDFIRADVTRIPLGGSVDTVVMNPPFgaqrR 125

                         90
                 ....*....|....*..
gi 447014802 109 HLD--------DIASVI 117
Cdd:COG2263  126 HADrpflekalEIAAVI 142
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 32-132 5.01e-04

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: 40.08  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802   32 MSPKKGRA-LDIGCGSGL-LVEKLASYYDEVVGIDISNQMLDLAKSKRQLTN----TVYLNMNAEQLNFNEKFDFIVSRT 105
Cdd:pfam08003 111 LSPLKGRTiLDVGCGNGYhMWRMLGEGAAMVVGIDPSELFLCQFEAVRKLLGndqrAHLLPLGIEQLPALAAFDTVFSMG 190

                          90       100
                  ....*....|....*....|....*..
gi 447014802  106 TFHHLDDIASVIQQMKELLNEEGRIVI 132
Cdd:pfam08003 191 VLYHRRSPLDHLLQLKDQLVKGGELVL 217
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
35-131 6.02e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 39.63  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  35 KKGRALDIGCGSGLLvEKLASYY--DEVVGIDISNQMLDLAK---SKRQLTNTV-YLNMNAEQLNFNEKFDFIVSRtTFH 108
Cdd:COG4076   35 PGDVVLDIGTGSGLL-SMLAARAgaKKVYAVEVNPDIAAVARriiAANGLSDRItVINADATDLDLPEKADVIISE-MLD 112

                         90       100
                 ....*....|....*....|....*..
gi 447014802 109 HL---DDIASVIQQ-MKELLNEEGRIV 131
Cdd:COG4076  113 TAlldEGQVPILNHaRKRLLKPGGRII 139
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
35-122 7.44e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 39.33  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  35 KKGRALDIGCGSGLLVEKLASYYDEVVGID---ISNQMLDLAKSKRQLTN--TVYLNMNAeqLNFNEKFDFIVSRTT--F 107
Cdd:PRK11207  30 KPGKTLDLGCGNGRNSLYLAANGFDVTAWDknpMSIANLERIKAAENLDNlhTAVVDLNN--LTFDGEYDFILSTVVlmF 107

                         90
                 ....*....|....*
gi 447014802 108 HHLDDIASVIQQMKE 122
Cdd:PRK11207 108 LEAKTIPGLIANMQR 122
PRK14968 PRK14968
putative methyltransferase; Provisional
 12-74 8.95e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.73  E-value: 8.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447014802  12 AEDydfvNELLNDYSFFVSNMspkkgRALDIGCGSGLLVEKLASYYDEVVGIDISNQMLDLAK 74
Cdd:PRK14968   9 AED----SFLLAENAVDKKGD-----RVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAK 62
PRK05785 PRK05785
hypothetical protein; Provisional
 34-120 1.49e-03

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 38.52  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  34 PKKGRALDIGCGSGLL---VEKLASYYdeVVGIDISNQMLDLAKSKRQLTNTVYlnmnaEQLNFNEK-FDFIVSRTTFHH 109
Cdd:PRK05785  50 GRPKKVLDVAAGKGELsyhFKKVFKYY--VVALDYAENMLKMNLVADDKVVGSF-----EALPFRDKsFDVVMSSFALHA 122

                         90
                 ....*....|.
gi 447014802 110 LDDIASVIQQM 120
Cdd:PRK05785 123 SDNIEKVIAEF 133
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
38-142 5.08e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.01  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802    38 RALDIGCGSGLLVEKLASYYD--EVVGIDISNQMLDLAKSK---RQLTNTVYL-NMNAEQLNFNEKFDFIVSRTTFHHLD 111
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERiraLGLQGRIRIfYRDSAKDPFPDTYDLVFGFEVIHHIK 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 447014802   112 DIASVIQQMKELLNEEGRIVILDNVSEVETP 142
Cdd:smart00828  82 DKMDLFSNISRHLKDGGHLVLADFIANLLSA 112
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 37-146 5.21e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 36.85  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447014802  37 GRALDIGCGSG----LLVEKLASyyDEVVGIDISNQMLDLAKSkrQLTNTVYLNMNAEQLNFNEKFDFIVSRTTFHHLDD 112
Cdd:PRK01683  33 RYVVDLGCGPGnsteLLVERWPA--ARITGIDSSPAMLAEARS--RLPDCQFVEADIASWQPPQALDLIFANASLQWLPD 108

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447014802 113 IASVIQQMKELLNEEGRIVIL--DNVSEvetpPTYV 146
Cdd:PRK01683 109 HLELFPRLVSLLAPGGVLAVQmpDNLDE----PSHV 140
 
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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