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Conserved domains on  [gi|340780664|pdb|3SM3|A]
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Chain A, SAM-dependent methyltransferases

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

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]; ...
 28-150 5.17e-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: 108.93  E-value: 5.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNqktggkAEFKVENASSLSFHDSSFDFAVM 107
Cdd:COG2226  20 LRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN------VEFVVGDAEDLPFPDGSFDLVIS 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3SM3_A      108 QAFLTSVPDPKersRIIKEVFRVLKPGAYLYLVEFGQNWHLKL 150
Cdd:COG2226  94 SFVLHHLPDPE---RALAEIARVLKPGGRLVVVDFSPPDLAEL 133
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 28-150 5.17e-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: 108.93  E-value: 5.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNqktggkAEFKVENASSLSFHDSSFDFAVM 107
Cdd:COG2226  20 LRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN------VEFVVGDAEDLPFPDGSFDLVIS 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3SM3_A      108 QAFLTSVPDPKersRIIKEVFRVLKPGAYLYLVEFGQNWHLKL 150
Cdd:COG2226  94 SFVLHHLPDPE---RALAEIARVLKPGGRLVVVDFSPPDLAEL 133
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 34-134 3.52e-28

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 102.64  E-value: 3.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         34 ILDIGCGSGKISLELASK-GYSVTGIDINSEAIRLAETAARSPGLNqktggkAEFKVENASSLSFHDSSFDFAVMQAFLT 112
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLN------VEFVQGDAEDLPFPDGSFDLVVSSGVLH 74

                          90       100
                  ....*....|....*....|..
3SM3_A        113 SVPDPkERSRIIKEVFRVLKPG 134
Cdd:pfam13649  75 HLPDP-DLEAALREIARVLKPG 95
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 29-205 7.61e-20

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 84.24  E-value: 7.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         29 QEDDEILDIGCGSGKISLELASKG---YSVTGIDINSEAIRLAETAARSPGlnqktggKAEFKVENASSLSFHDSSFDFA 105
Cdd:TIGR01934  38 FKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSELPL-------NIEFIQADAEALPFEDNSFDAV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        106 VMqAF-LTSVPDPKErsrIIKEVFRVLKPGAYLYLVEFGQ--NWHLKLYRKRYL-HDFPITkeeGSFLARDPETGE--TE 179
Cdd:TIGR01934 111 TI-AFgLRNVTDIQK---ALREMYRVLKPGGRLVILEFSKpaNALLKKFYKFYLkNVLPSI---GGLISKNAEAYTylPE 183

                         170       180
                  ....*....|....*....|....*.
3SM3_A        180 FIAHHFTEKELVFLLTDCRFEIDYFR 205
Cdd:TIGR01934 184 SIRAFPSQEELAAMLKEAGFEEVRYR 209
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 28-205 1.17e-18

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 81.35  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        28 LQEDDEILDIGCGSGKISLELASKGY---SVTGIDINSEAIRLAETAARSPGLnqktGGKAEFKVENASSLSFHDSSFDF 104
Cdd:PRK00216  49 VRPGDKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGMLAVGREKLRDLGL----SGNVEFVQGDAEALPFPDNSFDA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       105 AVMqAF-LTSVPDPKersRIIKEVFRVLKPGAYLYLVEFGQNW--HLKLYRKRYL-HDFPITkeeGSFLARDPETGE--T 178
Cdd:PRK00216 125 VTI-AFgLRNVPDID---KALREMYRVLKPGGRLVILEFSKPTnpPLKKAYDFYLfKVLPLI---GKLISKNAEAYSylA 197

                        170       180
                 ....*....|....*....|....*..
3SM3_A       179 EFIAHHFTEKELVFLLTDCRFEIDYFR 205
Cdd:PRK00216 198 ESIRAFPDQEELAAMLEEAGFERVRYR 224
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 34-140 5.77e-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: 73.62  E-value: 5.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       34 ILDIGCGSGKISLELAS-KGYSVTGIDINSEAIRLAETAARspglnQKTGGKAEFKVENASSLSF-HDSSFDFAVMQAFL 111
Cdd:cd02440   2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAA-----ALLADNVEVLKGDAEELPPeADESFDVIISDPPL 76

                        90       100
                ....*....|....*....|....*....
3SM3_A      112 TSVPDpkERSRIIKEVFRVLKPGAYLYLV 140
Cdd:cd02440  77 HHLVE--DLARFLEEARRLLKPGGVLVLT 103
rADc smart00650
Ribosomal RNA adenine dimethylases;
28-98 6.94e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.11  E-value: 6.94e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3SM3_A          28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSeaiRLAetaarsPGLNQKTGGKAEFKVENASSLSFH 98
Cdd:smart00650  11 LRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDP---RLA------PRLREKFAAADNLTVIHGDALKFD 72
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 28-150 5.17e-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: 108.93  E-value: 5.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNqktggkAEFKVENASSLSFHDSSFDFAVM 107
Cdd:COG2226  20 LRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLN------VEFVVGDAEDLPFPDGSFDLVIS 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3SM3_A      108 QAFLTSVPDPKersRIIKEVFRVLKPGAYLYLVEFGQNWHLKL 150
Cdd:COG2226  94 SFVLHHLPDPE---RALAEIARVLKPGGRLVVVDFSPPDLAEL 133
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 34-134 3.52e-28

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 102.64  E-value: 3.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         34 ILDIGCGSGKISLELASK-GYSVTGIDINSEAIRLAETAARSPGLNqktggkAEFKVENASSLSFHDSSFDFAVMQAFLT 112
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLN------VEFVQGDAEDLPFPDGSFDLVVSSGVLH 74

                          90       100
                  ....*....|....*....|..
3SM3_A        113 SVPDPkERSRIIKEVFRVLKPG 134
Cdd:pfam13649  75 HLPDP-DLEAALREIARVLKPG 95
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 19-139 1.19e-26

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: 99.71  E-value: 1.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       19 DLYPIIHNYLQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLnqktggkaEFKVENASSLSFH 98
Cdd:COG2227  13 RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV--------DFVQGDLEDLPLE 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
3SM3_A       99 DSSFDFAVMQAFLTSVPDPKErsrIIKEVFRVLKPGAYLYL 139
Cdd:COG2227  85 DGSFDLVICSEVLEHLPDPAA---LLRELARLLKPGGLLLL 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 35-139 8.94e-26

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 96.19  E-value: 8.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         35 LDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNqktggkaeFKVENASSLSFHDSSFDFAVMQAFLTSV 114
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT--------FVVGDAEDLPFPDNSFDLVLSSEVLHHV 72

                          90       100
                  ....*....|....*....|....*
3SM3_A        115 PDPkerSRIIKEVFRVLKPGAYLYL 139
Cdd:pfam08241  73 EDP---ERALREIARVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 5-140 3.51e-21

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 87.28  E-value: 3.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        5 YWEKVSGKNIPSSLDLYPIIHNYLQEDDEILDIGCGSGKISLELASK-GYSVTGIDINSEAIRLAETAARSPGLnqktgG 83
Cdd:COG0500   1 PWDSYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGL-----G 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
3SM3_A       84 KAEFKVENAS-SLSFHDSSFDFAVMQAFLTSVPdPKERSRIIKEVFRVLKPGAYLYLV 140
Cdd:COG0500  76 NVEFLVADLAeLDPLPAESFDLVVAFGVLHHLP-PEEREALLRELARALKPGGVLLLS 132
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 29-205 7.61e-20

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 84.24  E-value: 7.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         29 QEDDEILDIGCGSGKISLELASKG---YSVTGIDINSEAIRLAETAARSPGlnqktggKAEFKVENASSLSFHDSSFDFA 105
Cdd:TIGR01934  38 FKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSELPL-------NIEFIQADAEALPFEDNSFDAV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        106 VMqAF-LTSVPDPKErsrIIKEVFRVLKPGAYLYLVEFGQ--NWHLKLYRKRYL-HDFPITkeeGSFLARDPETGE--TE 179
Cdd:TIGR01934 111 TI-AFgLRNVTDIQK---ALREMYRVLKPGGRLVILEFSKpaNALLKKFYKFYLkNVLPSI---GGLISKNAEAYTylPE 183

                         170       180
                  ....*....|....*....|....*.
3SM3_A        180 FIAHHFTEKELVFLLTDCRFEIDYFR 205
Cdd:TIGR01934 184 SIRAFPSQEELAAMLKEAGFEEVRYR 209
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 28-205 1.17e-18

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 81.35  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        28 LQEDDEILDIGCGSGKISLELASKGY---SVTGIDINSEAIRLAETAARSPGLnqktGGKAEFKVENASSLSFHDSSFDF 104
Cdd:PRK00216  49 VRPGDKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGMLAVGREKLRDLGL----SGNVEFVQGDAEALPFPDNSFDA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       105 AVMqAF-LTSVPDPKersRIIKEVFRVLKPGAYLYLVEFGQNW--HLKLYRKRYL-HDFPITkeeGSFLARDPETGE--T 178
Cdd:PRK00216 125 VTI-AFgLRNVPDID---KALREMYRVLKPGGRLVILEFSKPTnpPLKKAYDFYLfKVLPLI---GKLISKNAEAYSylA 197

                        170       180
                 ....*....|....*....|....*..
3SM3_A       179 EFIAHHFTEKELVFLLTDCRFEIDYFR 205
Cdd:PRK00216 198 ESIRAFPDQEELAAMLEEAGFERVRYR 224
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 30-142 2.68e-17

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 75.92  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         30 EDDEILDIGCGSGKISLELASKGYS---VTGIDINSEAIRLAETAARSPGLNqktggKAEFKVENASSL--SFHDSSFDF 104
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARENAQKLGFD-----NVEFEQGDIEELpeLLEDDKFDV 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
3SM3_A        105 AVMQAFLTSVPDPKErsrIIKEVFRVLKPGAYLYLVEF 142
Cdd:pfam13847  78 VISNCVLNHIPDPDK---VLQEILRVLKPGGRLIISDP 112
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 34-140 5.77e-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: 73.62  E-value: 5.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       34 ILDIGCGSGKISLELAS-KGYSVTGIDINSEAIRLAETAARspglnQKTGGKAEFKVENASSLSF-HDSSFDFAVMQAFL 111
Cdd:cd02440   2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAA-----ALLADNVEVLKGDAEELPPeADESFDVIISDPPL 76

                        90       100
                ....*....|....*....|....*....
3SM3_A      112 TSVPDpkERSRIIKEVFRVLKPGAYLYLV 140
Cdd:cd02440  77 HHLVE--DLARFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
34-158 1.95e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 74.26  E-value: 1.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       34 ILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAEtaarspglnqKTGGKAEFKVENASSLSFHDSSFDFAVMQAFLTS 113
Cdd:COG4976  50 VLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----------EKGVYDRLLVADLADLAEPDGRFDLIVAADVLTY 119

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
3SM3_A      114 VPDPKersRIIKEVFRVLKPGAYLYL-VEFGQNWHLKLYRKRYLHD 158
Cdd:COG4976 120 LGDLA---AVFAGVARALKPGGLFIFsVEDADGSGRYAHSLDYVRD 162
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 28-139 2.01e-16

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 73.81  E-value: 2.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       28 LQEDDEILDIGCGSGKISLELASK-GYSVTGIDINSEAIRLAETAARSPGLNqktgGKAEFKVENASSLSFhDSSFDFAV 106
Cdd:COG2230  49 LKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLA----DRVEVRLADYRDLPA-DGQFDAIV 123

                        90       100       110
                ....*....|....*....|....*....|...
3SM3_A      107 MQAFLTSVPdPKERSRIIKEVFRVLKPGAYLYL 139
Cdd:COG2230 124 SIGMFEHVG-PENYPAYFAKVARLLKPGGRLLL 155
PRK08317 PRK08317
hypothetical protein; Provisional
 28-142 3.89e-15

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 71.89  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        28 LQEDDEILDIGCGSGKISLELA---SKGYSVTGIDINSEAIRLAETAARSPGLNqktggkAEFKVENASSLSFHDSSFDF 104
Cdd:PRK08317  17 VQPGDRVLDVGCGPGNDARELArrvGPEGRVVGIDRSEAMLALAKERAAGLGPN------VEFVRGDADGLPFPDGSFDA 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
3SM3_A       105 AV-MQAFlTSVPDPkerSRIIKEVFRVLKPGAYLYLVEF 142
Cdd:PRK08317  91 VRsDRVL-QHLEDP---ARALAEIARVLRPGGRVVVLDT 125
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
34-141 1.58e-14

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 67.16  E-value: 1.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       34 ILDIGCGSGKISLELASK--GYSVTGIDINSEAIRLAetAARSPGLnqktggkaEFKVENASSLSFhDSSFDFAVMQAFL 111
Cdd:COG4106   5 VLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARA--RARLPNV--------RFVVADLRDLDP-PEPFDLVVSNAAL 73

                        90       100       110
                ....*....|....*....|....*....|
3SM3_A      112 TSVPDPKersRIIKEVFRVLKPGAYLYLVE 141
Cdd:COG4106  74 HWLPDHA---ALLARLAAALAPGGVLAVQV 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 27-160 2.95e-14

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 67.84  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         27 YLQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAetaarspglnqktGGKAEFKVENASSLSFHDSSFDFAV 106
Cdd:pfam13489  19 KLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERA-------------LLNVRFDQFDEQEAAVPAGKFDVIV 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
3SM3_A        107 MQAFLTSVPDPkerSRIIKEVFRVLKPGAYLYLVEFGQNWHLKLYRKRYLHDFP 160
Cdd:pfam13489  86 AREVLEHVPDP---PALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRP 136
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
34-174 2.34e-13

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 67.08  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         34 ILDIGCGSGKIS---LELASKGYSVTGIDINSEAIRLAETAARSPGLNQktggkAEFKVENASSLSFHDSSFDFAVMQAF 110
Cdd:pfam01209  46 FLDVAGGTGDWTfglSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYN-----IEFLQGNAEELPFEDDSFDIVTISFG 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
3SM3_A        111 LTSVPDpkeRSRIIKEVFRVLKPGAYLYLVEFGQNwHLKLYRKRY-LHDFPITKEEGSFLARDPE 174
Cdd:pfam01209 121 LRNFPD---YLKVLKEAFRVLKPGGRVVCLEFSKP-ENPLLSQAYeLYFKYVMPFMGKMFAKSYK 181
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 28-137 4.03e-12

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: 62.27  E-value: 4.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNqktggKAEFKVENASSLSFHDSSFDFAVM 107
Cdd:COG1041  24 AKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYE-----DADVIRGDARDLPLADESVDAIVT 98

                        90       100       110
                ....*....|....*....|....*....|....*.
3SM3_A      108 -----QAFLTSVPDPKER-SRIIKEVFRVLKPGAYL 137
Cdd:COG1041  99 dppygRSSKISGEELLELyEKALEEAARVLKPGGRV 134
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 32-145 2.64e-11

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 61.45  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        32 DEILDIGCGSGKISLELASKGYS---VTGIDINSEaiRLAETAARSPGLNQKTGGKAEFKVENASSLSFHDSSFDFAVMQ 108
Cdd:PLN02233  75 DRVLDLCCGSGDLAFLLSEKVGSdgkVMGLDFSSE--QLAVAASRQELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMG 152

                         90       100       110
                 ....*....|....*....|....*....|....*..
3SM3_A       109 AFLTSVPDpkeRSRIIKEVFRVLKPGAYLYLVEFGQN 145
Cdd:PLN02233 153 YGLRNVVD---RLKAMQEMYRVLKPGSRVSILDFNKS 186
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 29-153 2.86e-11

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: 60.59  E-value: 2.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       29 QEDDEILDIGCGSGKISLELA--SKGYSVTGIDINSEAIRLAETAARSPGLNQktggkAEFKVENASSlSFHDSSFDFAV 106
Cdd:COG2813  48 PLGGRVLDLGCGYGVIGLALAkrNPEARVTLVDVNARAVELARANAAANGLEN-----VEVLWSDGLS-GVPDGSFDLIL 121

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
3SM3_A      107 M-----QAFLTsvpDPKERSRIIKEVFRVLKPGAYLYLVefGQNwHLKLYRK 153
Cdd:COG2813 122 SnppfhAGRAV---DKEVAHALIADAARHLRPGGELWLV--ANR-HLPYERK 167
PRK14968 PRK14968
putative methyltransferase; Provisional
 29-140 9.87e-11

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 58.76  E-value: 9.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        29 QEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNqktggKAEFKVENASSLS-FHDSSFDFAVM 107
Cdd:PRK14968  22 KKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIR-----NNGVEVIRSDLFEpFRGDKFDVILF 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
3SM3_A       108 QA-FLTSVPDPKER-----------------SRIIKEVFRVLKPGAYLYLV 140
Cdd:PRK14968  97 NPpYLPTEEEEEWDdwlnyalsggkdgreviDRFLDEVGRYLKPGGRILLL 147
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 35-137 2.11e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.84  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         35 LDIGCGSGKISLELASK--GYSVTGIDINSEAIRLAetAARSPGLNQKTGGKAEFKVENASSLsfHDSSFDFAVMQAFLT 112
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAA--RERLAALGLLNAVRVELFQLDLGEL--DPGSFDVVVASNVLH 76

                          90       100
                  ....*....|....*....|....*
3SM3_A        113 SVPDPKErsrIIKEVFRVLKPGAYL 137
Cdd:pfam08242  77 HLADPRA---VLRNIRRLLKPGGVL 98
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 34-151 3.16e-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: 58.07  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         34 ILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAArspglnQKTGGKAEFKVENASSLSF-HDSSFDFAVMQAFLT 112
Cdd:TIGR01983  50 VLDVGCGGGLLSEPLARLGANVTGIDASEENIEVAKLHA------KKDPLQIDYRCTTVEDLAEkKAGSFDVVTCMEVLE 123

                          90       100       110
                  ....*....|....*....|....*....|....*....
3SM3_A        113 SVPDPkerSRIIKEVFRVLKPGAYLYLVEFGQNWHLKLY 151
Cdd:TIGR01983 124 HVPDP---QAFIRACAQLLKPGGILFFSTINRTPKSYLL 159
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 1-82 2.09e-09

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 56.49  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         1 MPESYWEKVSGKNIPSS--LDLYPIIHNylqedDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLN 78
Cdd:PRK12335  94 KPEDYFHKKYNLTATHSevLEAVQTVKP-----GKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLN 168


                 ....
3SM3_A        79 QKTG 82
Cdd:PRK12335 169 IRTG 172
PLN02244 PLN02244
tocopherol O-methyltransferase
 34-140 6.63e-09

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 55.14  E-value: 6.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        34 ILDIGCGSGKISLELASK-GYSVTGIDINSEAIRLAETAARSPGLnqktGGKAEFKVENASSLSFHDSSFDFAVMQAFLT 112
Cdd:PLN02244 122 IVDVGCGIGGSSRYLARKyGANVKGITLSPVQAARANALAAAQGL----SDKVSFQVADALNQPFEDGQFDLVWSMESGE 197

                         90       100
                 ....*....|....*....|....*...
3SM3_A       113 SVPDpkeRSRIIKEVFRVLKPGAYLYLV 140
Cdd:PLN02244 198 HMPD---KRKFVQELARVAAPGGRIIIV 222
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 26-158 8.68e-09

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 54.53  E-value: 8.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        26 NYLQEDDE-ILDIGCGSGKISLELA-----SKGYSVTGIDINSEAIRLAetAARSPGLnqktggkaEFKVENASSLSFHD 99
Cdd:PRK11088  80 ERLDEKATaLLDIGCGEGYYTHALAdalpeITTMQLFGLDISKVAIKYA--AKRYPQV--------TFCVASSHRLPFAD 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3SM3_A       100 SSFDFAVmqafltsvpdpkersRI-----IKEVFRVLKPGAYLYLVEFGQNWHLKL----YRKRYLHD 158
Cdd:PRK11088 150 QSLDAII---------------RIyapckAEELARVVKPGGIVITVTPGPRHLFELkgliYDEVRLHA 202
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 27-106 9.23e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.07  E-value: 9.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        27 YLQEDDE-----ILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNqktgGKAEFKVENASSLSfhdSS 101
Cdd:PRK07580  55 WLPADGDltglrILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLA----GNITFEVGDLESLL---GR 127


                 ....*
3SM3_A       102 FDFAV 106
Cdd:PRK07580 128 FDTVV 132
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
19-160 1.01e-08

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 54.20  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        19 DLYPIIHNYLQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNQKTggkaEFKVENASSLSFH 98
Cdd:PRK11036  33 DLDRLLAELPPRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNM----QFIHCAAQDIAQH 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
3SM3_A        99 -DSSFDFAVMQAFLTSVPDPKErsrIIKEVFRVLKPGAYLYLVEFgqNWHLKLYRKRYLHDFP 160
Cdd:PRK11036 109 lETPVDLILFHAVLEWVADPKS---VLQTLWSVLRPGGALSLMFY--NANGLLMHNMVAGNFD 166
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 34-160 2.41e-08

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: 52.84  E-value: 2.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       34 ILDIGCGSGKISLELASKGY--SVTGIDINSEAIRLA-ETAARSPgLNQKtggkaeFKVENAS----SLSFHDSSFDFAV 106
Cdd:COG4123  41 VLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELArRNVALNG-LEDR------ITVIHGDlkefAAELPPGSFDLVV 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A      107 M-------QAFLTSVPDPKERSR---------IIKEVFRVLKPGAYLYLV-------EF-----GQNWHLKlyRKRYLHD 158
Cdd:COG4123 114 SnppyfkaGSGRKSPDEARAIARhedaltledLIRAAARLLKPGGRFALIhpaerlaEIlaalrKYGLGPK--RLRPVHP 191


                ..
3SM3_A      159 FP 160
Cdd:COG4123 192 RP 193
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 34-144 2.57e-08

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: 52.67  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         34 ILDIGCGSGKISLELASKG--YSVTGIDINSEAIRLAETAArspglnqktGGKAEFKVENASSLSFHDSSFDFAVMQAFL 111
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKL---------SENVQFICGDAEKLPLEDSSFDLIVSNLAL 108

                          90       100       110
                  ....*....|....*....|....*....|...
3SM3_A        112 TSVPDPKersRIIKEVFRVLKPGAYLYLVEFGQ 144
Cdd:TIGR02072 109 QWCDDLS---QALSELARVLKPGGLLAFSTFGP 138
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
35-136 3.72e-08

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 51.66  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        35 LDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNQktggkAEFKVENASSLSFhDSSFDF---AVMQAFL 111
Cdd:PRK11207  35 LDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDN-----LHTAVVDLNNLTF-DGEYDFilsTVVLMFL 108

                         90       100
                 ....*....|....*....|....*
3SM3_A       112 tsvpDPKERSRIIKEVFRVLKPGAY 136
Cdd:PRK11207 109 ----EAKTIPGLIANMQRCTKPGGY 129
PRK06202 PRK06202
hypothetical protein; Provisional
 34-111 1.55e-07

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 50.38  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        34 ILDIGCGSGKISLELAS----KGYS--VTGIDINSEAIRLAETAARSPGLNqktggkaeFKVENASSLSFHDSSFDFAVM 107
Cdd:PRK06202  64 LLDIGCGGGDLAIDLARwarrDGLRleVTAIDPDPRAVAFARANPRRPGVT--------FRQAVSDELVAEGERFDVVTS 135


                 ....
3SM3_A       108 QAFL 111
Cdd:PRK06202 136 NHFL 139
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 28-92 2.15e-07

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 50.56  E-value: 2.15e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3SM3_A       28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNQktggkAEFKVENA 92
Cdd:COG2265 231 LTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKN-----VEFVAGDL 290
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
30-107 5.20e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 48.36  E-value: 5.20e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3SM3_A       30 EDDEILDIGCGSGKISLELASKG-YSVTGIDINSEAIRLAETAARspglnqKTGGKAEFKVENASSLSFhDSSFDFAVM 107
Cdd:COG2263  45 EGKTVLDLGCGTGMLAIGAALLGaKKVVGVDIDPEALEIARENAE------RLGVRVDFIRADVTRIPL-GGSVDTVVM 116
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 31-140 1.02e-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: 47.20  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         31 DDEILDIGCGSGKISLELASKG--YSVTGIDINSEAIRLAETAARSPGLNqktggKAEFKVENASSlSFHDSSFDFAVM- 107
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLE-----NGEVVASDVYS-GVEDGKFDLIISn 105

                          90       100       110
                  ....*....|....*....|....*....|....*....
3SM3_A        108 ------QAFLTSVPDpkersRIIKEVFRVLKPGAYLYLV 140
Cdd:pfam05175 106 ppfhagLATTYNVAQ-----RFIADAKRHLRPGGELWIV 139
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 23-145 1.09e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 48.23  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        23 IIHNYLQEDDEILDIGCGSGKISLELAS--KGYSVTGIDINSEAIRLAETaarspglNQKTGGKAEFKVENASSLS-FHD 99
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIALALAKerPDAEVTAVDISPEALAVARR-------NAKHGLGARVEFLQGDWFEpLPG 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3SM3_A       100 SSFDFAV-------------MQ----------AfLTSVPDPKE--RsRIIKEVFRVLKPGAYLYLvEFGQN 145
Cdd:PRK09328 174 GRFDLIVsnppyipeadihlLQpevrdhephlA-LFGGEDGLDfyR-RIIEQAPRYLKPGGWLLL-EIGYD 241
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 28-78 1.61e-06

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 45.78  E-value: 1.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
3SM3_A         28 LQEDDEILDIGCGSGKISLELASK--GYSVTGIDINSEAIRLAETAARSPGLN 78
Cdd:TIGR02469  17 LRPGDVLWDIGAGTGSVTIEAARLvpNGRVYAIERNPEALDLIERNLRRFGVS 69
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 32-156 2.36e-06

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: 47.35  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         32 DEILDIGCGSGKISLELAS--KGYSVTGIDINSEAIRLAETAARSPGLNQ------------KTGGKAEFKVEN-----A 92
Cdd:TIGR00536 116 LHILDLGTGSGCIALALAYefPNAEVIAVDISPDALAVAEENAEKNQLEHrvefiqsnlfepLAGQKIDIIVSNppyidE 195

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
3SM3_A         93 SSLSFHDSSFDFAVMQAFLTSVPDPKERSRIIKEVFRVLKPGAYLyLVEFGqNWHLKLYrKRYL 156
Cdd:TIGR00536 196 EDLADLPNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFL-VCEIG-NWQQKSL-KELL 256
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 38-166 3.34e-06

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 46.27  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         38 GCGSGKISLELASKGYSVTGIDINSEAIR-LAETAARSPGLNQKTGGKaEFKVEN------------ASSLSFHDSSFDf 104
Cdd:pfam05724  45 LCGKALDMVWLAEQGHFVVGVEISELAVEkFFAEAGLSPPITELSGFK-EYSSGNislycgdfftlpREELGKFDLIYD- 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
3SM3_A        105 avmQAFLTSVPdPKERSRIIKEVFRVLKPGAYLYLVEFgqnwhlklyrkrylhDFPITKEEG 166
Cdd:pfam05724 123 ---RAALCALP-PEMRPRYAKQMYELLPPGGRGLLITL---------------DYPQTDHEG 165
arsM PRK11873
arsenite methyltransferase;
28-138 3.44e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 46.87  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        28 LQEDDEILDIGCGSGkISLELASK--GYS--VTGIDINSEAIRLAETAARSPGLNQktggkAEFKVENASSLSFHDSSFD 103
Cdd:PRK11873  75 LKPGETVLDLGSGGG-FDCFLAARrvGPTgkVIGVDMTPEMLAKARANARKAGYTN-----VEFRLGEIEALPVADNSVD 148

                         90       100       110
                 ....*....|....*....|....*....|....*
3SM3_A       104 FAVMQAFLTSVPDpKERsrIIKEVFRVLKPGAYLY 138
Cdd:PRK11873 149 VIISNCVINLSPD-KER--VFKEAFRVLKPGGRFA 180
TehB pfam03848
Tellurite resistance protein TehB;
33-140 9.46e-06

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 44.84  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         33 EILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNQKTGgkaefKVENASSLSFhDSSFDF---AVMQA 109
Cdd:pfam03848  33 KVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDNIHT-----ALYDINNATI-DENYDFilsTVVLM 106

                          90       100       110
                  ....*....|....*....|....*....|.
3SM3_A        110 FLtsvpDPKERSRIIKEVFRVLKPGAYLYLV 140
Cdd:pfam03848 107 FL----EPERIPGIIANMQECTNPGGYNLIV 133
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 28-73 2.04e-05

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 44.77  E-value: 2.04e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
3SM3_A       28 LQEDDEILDIGCGSGKISLE--LASKGYSVTGIDINSEAIRLAETAAR 73
Cdd:COG2242 245 LRPGDVLWDIGAGSGSVSIEaaRLAPGGRVYAIERDPERAALIRANAR 292
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 34-69 2.73e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.99  E-value: 2.73e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
3SM3_A       34 ILDIGCGSGKISLELAS--KGYSVTGIDINSEAIRLAE 69
Cdd:COG2890 116 VLDLGTGSGAIALALAKerPDARVTAVDISPDALAVAR 153
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 30-140 4.20e-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: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         30 EDDEILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLN---------QKTGGKAEFKVENASSLSFHD- 99
Cdd:TIGR00537  19 KPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVGldvvmtdlfKGVRGKFDVILFNPPYLPLEDd 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
3SM3_A        100 ----SSFDFA---------VMQAFLTSVPDP-KERSRII---------KEVFRVLKPGAYLYLV 140
Cdd:TIGR00537  99 lrrgDWLDVAidggkdgrkVIDRFLDELPEIlKEGGRVQliqsslngePDTFDKLDERGFRYEI 162
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
36-79 5.12e-05

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 43.32  E-value: 5.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
3SM3_A        36 DIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNQ 79
Cdd:PRK03522 179 DLFCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTN 222
rADc smart00650
Ribosomal RNA adenine dimethylases;
28-98 6.94e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.11  E-value: 6.94e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3SM3_A          28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSeaiRLAetaarsPGLNQKTGGKAEFKVENASSLSFH 98
Cdd:smart00650  11 LRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDP---RLA------PRLREKFAAADNLTVIHGDALKFD 72
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
26-139 8.96e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 42.45  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        26 NYLQEDDEILDIGCGSGkIsLELASKGY---SVTGIDINSEAIRLAETAARspgLNQktggkaefkVENASSLSFHDSSF 102
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSG-I-LAIAAAKLgakKVLAVDIDPQAVEAARENAE---LNG---------VELNVYLPQGDLKA 180

                         90       100       110
                 ....*....|....*....|....*....|....*...
3SM3_A       103 DFAVmqA-FLTSVPDpkersRIIKEVFRVLKPGAYLYL 139
Cdd:PRK00517 181 DVIV--AnILANPLL-----ELAPDLARLLKPGGRLIL 211
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 57-145 1.01e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 41.60  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        57 GIDINSEAIRLAETaarSPGLNQKTGGKA-EFKVENASSLSFHDSSFDFAVMQAFLTSVPDpkeRSRIIKEVFRVLKPGA 135
Cdd:PLN02232   2 GLDFSSEQLAVAAT---RQSLKARSCYKCiEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVD---RLRAMKEMYRVLKPGS 75

                         90
                 ....*....|
3SM3_A       136 YLYLVEFGQN 145
Cdd:PLN02232  76 RVSILDFNKS 85
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
95-200 1.45e-04

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 41.01  E-value: 1.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A       95 LSFHDSSFDFAVMQAFLTSVPDPkERSRIIKEVFRVLKPGAYLYLV--------EFGQNWHLKLYRKRYLHDFPITKEEG 166
Cdd:COG4627  40 LPFPDNSVDAIYSSHVLEHLDYE-EAPLALKECYRVLKPGGILRIVvpdlehvaRLYLAEYDAALDVAELRLAGPIDPLG 118

                        90       100       110
                ....*....|....*....|....*....|....
3SM3_A      167 SFLARDPETGETEFIAHHFTEKELVFLLTDCRFE 200
Cdd:COG4627 119 IILGERLAGLAARHSVLFRTGFTRLALTARRSAA 152
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 29-103 3.26e-04

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 40.42  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         29 QEDDEILDIGCGSGKISLELASKG-------------YSVTGIDINSEAIRLAETAARSPGLnqktGGKAEFKVENASSL 95
Cdd:pfam01170  27 KPGDPLLDPMCGSGTILIEAALMGaniapgkfdarvrAPLYGSDIDRRMVQGARLNAENAGV----GDLIEFVQADAADL 102


                  ....*...
3SM3_A         96 SFHDSSFD 103
Cdd:pfam01170 103 PLLEGSVD 110
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 23-130 3.66e-04

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: 40.13  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A         23 IIHNYLQEDDEILDIGCGSGKIsLELASKGYSVTGIDINSEAIRLAETAARSPGLNQktgGKAEFKVENasslsFHDSSF 102
Cdd:pfam07021   6 YILEWIPPGSRVLDLGCGDGTL-LYLLKEEKGVDGYGIELDAAGVAECVAKGLYVIQ---GDLDEGLEH-----FPDKSF 76

                          90       100
                  ....*....|....*....|....*...
3SM3_A        103 DFAVMQAFLTSVPDPKersRIIKEVFRV 130
Cdd:pfam07021  77 DYVILSQTLQATRNPR---EVLDEMLRI 101
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 27-79 5.93e-04

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 39.87  E-value: 5.93e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
3SM3_A       27 YLQEDDE-----ILDIGCGSGKISLELASKG-YSVTGIDINSEAIRLAETAARspgLNQ 79
Cdd:COG3897  62 YLLDHPEvagkrVLELGCGLGLVGIAAAKAGaADVTATDYDPEALAALRLNAA---LNG 117
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
27-73 7.34e-04

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 39.77  E-value: 7.34e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
3SM3_A       27 YLQEDDEILDIGCGSGKISLeLASK-GYS-VTGIDINSEAIRLA-ETAAR 73
Cdd:COG2264 145 LLKPGKTVLDVGCGSGILAI-AAAKlGAKrVLAVDIDPVAVEAArENAEL 193
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 33-119 1.11e-03

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 39.33  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        33 EILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAArspGLNQKTgGKAEFKVENASSLSFHDSSFDFAVMQAFLT 112
Cdd:PLN02396 134 KFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHA---DMDPVT-STIEYLCTTAEKLADEGRKFDAVLSLEVIE 209


                 ....*..
3SM3_A       113 SVPDPKE 119
Cdd:PLN02396 210 HVANPAE 216
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 26-73 1.14e-03

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: 39.17  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
3SM3_A         26 NYLQEDDEILDIGCGSGKIS---LELASKgySVTGIDINSEAIRLA-ETAAR 73
Cdd:pfam06325 157 RLVKPGESVLDVGCGSGILAiaaLKLGAK--KVVGVDIDPVAVRAAkENAEL 206
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 34-96 1.17e-03

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 39.46  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
3SM3_A        34 ILDIGCGSGKISLELASKGYSVTGIDINSEAIRLAETAARSPGLNQKTGGKAEFKVENASSLS 96
Cdd:PLN02585 148 VCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAERRAKEALAALPPEVLPKFEANDLESLS 210
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 28-78 2.45e-03

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 38.18  E-value: 2.45e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
3SM3_A       28 LQEDDEILDIGCGSGKISLELASKGYSVTGIDINSEAI-RLAETAARSPGLN 78
Cdd:COG0030  35 ITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAaILRETFAAYPNLT 86
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 27-154 3.26e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 37.64  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3SM3_A        27 YLQEDDEILDIGCGSGKISLELASK-GYSVTGIDINSEAIRLAEtaarspgLNQKTGGKAEFKVENASSLSFHDSSFDFA 105
Cdd:PTZ00098  49 ELNENSKVLDIGSGLGGGCKYINEKyGAHVHGVDICEKMVNIAK-------LRNSDKNKIEFEANDILKKDFPENTFDMI 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
3SM3_A       106 VMQAFLTSVPdPKERSRIIKEVFRVLKPGAYLYLVEFG----QNW--HLKLYRKR 154
Cdd:PTZ00098 122 YSRDAILHLS-YADKKKLFEKCYKWLKPNGILLITDYCadkiENWdeEFKAYIKK 175
 
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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