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Conserved domains on  [gi|1225045451|ref|WP_093059469|]
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class I SAM-dependent methyltransferase [Variovorax sp. YR634]

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]; ...
 169-285 3.94e-21

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: 88.13  E-value: 3.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAypESSFVGFDYHAPSIERARETARKAGVddekRLRFQVASAKD--FPGENYDLVAV 246
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL----NVEFVVGDAEDlpFPDGSFDLVIS 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1225045451 247 FDCLHDMGDPVGAAAHVRRSLKPQGTWMIVEPFANDRLE 285
Cdd:COG2226    94 SFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 169-285 3.94e-21

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: 88.13  E-value: 3.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAypESSFVGFDYHAPSIERARETARKAGVddekRLRFQVASAKD--FPGENYDLVAV 246
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL----NVEFVVGDAEDlpFPDGSFDLVIS 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1225045451 247 FDCLHDMGDPVGAAAHVRRSLKPQGTWMIVEPFANDRLE 285
Cdd:COG2226    94 SFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 175-271 2.96e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.06  E-value: 2.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 175 VADVGCGHGASTLLMAQAYpESSFVGFDYHAPSIERARETARKAGVddekRLRFQVASAKD--FPGENYDLVAVFDCLHD 252
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL----NVEFVQGDAEDlpFPDGSFDLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 1225045451 253 MGDP--VGAAAHVRRSLKPQG 271
Cdd:pfam13649  76 LPDPdlEAALREIARVLKPGG 96
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
174-342 3.09e-11

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 62.43  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451  174 RVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGVDDEKRLRFQVASAKDFPGeNYDLVAVFDCLHDM 253
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPD-TYDLVFGFEVIHHI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451  254 GDPVGAAAHVRRSLKPQGTWMIVEPFANDRLEDNInPVGRVFYSASSFICTPASR-----------SQEVGLCLGAQAGE 322
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAIEH-EETTSYLVTREEWAELLARnnlrvvegvdaSLEIANFLYDPGFE 159

                          170       180
                   ....*....|....*....|....*..
gi 1225045451  323 ARLREV-------VTQGGFSHFRRASE 342
Cdd:smart00828 160 DNLERLyqddldeVTKRHFRGIANLGK 186
PRK08317 PRK08317
hypothetical protein; Provisional
 169-278 8.23e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 58.41  E-value: 8.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAY-PESSFVGFDYHAPSIERAREtaRKAGVDDEKRLRFQVASAKDFPGENYDLVA-- 245
Cdd:PRK08317   17 VQPGDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDADGLPFPDGSFDAVRsd 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1225045451 246 -VFDCLHdmgDPVGAAAHVRRSLKPQGTWMIVEP 278
Cdd:PRK08317   95 rVLQHLE---DPARALAEIARVLRPGGRVVVLDT 125
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 174-271 6.15e-08

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 50.12  E-value: 6.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 174 RVADVGCGHGASTLLMAQAYPEsSFVGFDYHAPSIERARETARKAGVDdekRLRFQVASAKDFP---GENYDLVAVFDCL 250
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA-RVTGVDISPVALELARKAAAALLAD---NVEVLKGDAEELPpeaDESFDVIISDPPL 76

                          90       100
                  ....*....|....*....|..
gi 1225045451 251 HD-MGDPVGAAAHVRRSLKPQG 271
Cdd:cd02440    77 HHlVEDLARFLEEARRLLKPGG 98
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
 175-220 4.12e-05

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 43.89  E-value: 4.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1225045451 175 VADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGV 220
Cdd:TIGR00091  20 HLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGL 65
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 169-285 3.94e-21

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: 88.13  E-value: 3.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAypESSFVGFDYHAPSIERARETARKAGVddekRLRFQVASAKD--FPGENYDLVAV 246
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL----NVEFVVGDAEDlpFPDGSFDLVIS 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1225045451 247 FDCLHDMGDPVGAAAHVRRSLKPQGTWMIVEPFANDRLE 285
Cdd:COG2226    94 SFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
171-277 8.67e-21

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 85.65  E-value: 8.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 171 RGARVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARkagvddekRLRFQVASAKDF-PGENYDLVAVFDC 249
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP--------NVRFVVADLRDLdPPEPFDLVVSNAA 72

                          90       100
                  ....*....|....*....|....*...
gi 1225045451 250 LHDMGDPVGAAAHVRRSLKPQGTWMIVE 277
Cdd:COG4106    73 LHWLPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 160-286 5.84e-20

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 86.51  E-value: 5.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 160 PALEGIEPLLKRGARVADVGCGHGASTLLMAQAYpESSFVGFDYHAPSIERARETARKAGVDdekRLRFQVASA---KDF 236
Cdd:COG0500    15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLG---NVEFLVADLaelDPL 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1225045451 237 PGENYDLVAVFDCLHDM--GDPVGAAAHVRRSLKPQGTWMIVEPFANDRLED 286
Cdd:COG0500    91 PAESFDLVVAFGVLHHLppEEREALLRELARALKPGGVLLLSASDAAAALSL 142
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 158-278 2.41e-18

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: 80.06  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 158 WIPALEG-IEPLLKRGARVADVGCGHGASTLLMAQAypESSFVGFDYHAPSIERARETARKAGVDdekrlrFQVASAKD- 235
Cdd:COG2227    10 WDRRLAAlLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNVD------FVQGDLEDl 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1225045451 236 -FPGENYDLVAVFDCLHDMGDPVGAAAHVRRSLKPQGTWMIVEP 278
Cdd:COG2227    82 pLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTP 125
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 175-271 2.96e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.06  E-value: 2.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 175 VADVGCGHGASTLLMAQAYpESSFVGFDYHAPSIERARETARKAGVddekRLRFQVASAKD--FPGENYDLVAVFDCLHD 252
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL----NVEFVQGDAEDlpFPDGSFDLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 1225045451 253 MGDP--VGAAAHVRRSLKPQG 271
Cdd:pfam13649  76 LPDPdlEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 177-271 1.32e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 74.33  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 177 DVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGVDDEKRLRFQVASAKDFPGENYDLVAVFDCLHDMGDP 256
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLADP 81

                          90
                  ....*....|....*
gi 1225045451 257 VGAAAHVRRSLKPQG 271
Cdd:pfam08242  82 RAVLRNIRRLLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 169-278 7.56e-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: 7.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAYpESSFVGFDYHAPSIERARETARKAGVDDekRLRFQVASAKDFPGEN-YDLVAVF 247
Cdd:COG2230    49 LKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLAD--RVEVRLADYRDLPADGqFDAIVSI 125

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1225045451 248 DCLHDMGDPVGAA--AHVRRSLKPQGTWMIVEP 278
Cdd:COG2230   126 GMFEHVGPENYPAyfAKVARLLKPGGRLLLHTP 158
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 169-288 4.01e-15

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 71.68  E-value: 4.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQ-AYPESSFVGFDYHAPSIERARETARKAGVDdekRLRFQVASAKDFP----GENYDL 243
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLGFD---NVEFEQGDIEELPelleDDKFDV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1225045451 244 VAVFDCLHDMGDPVGAAAHVRRSLKPQGTWMIVEPFANDRLEDNI 288
Cdd:pfam13847  78 VISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHV 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 177-271 2.08e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 62.30  E-value: 2.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 177 DVGCGHGASTLLMAQAYPEssFVGFDYHAPSIERARETARKAGVDdekrlrFQVASAKD--FPGENYDLVAVFDCLHDMG 254
Cdd:pfam08241   2 DVGCGTGLLTELLARLGAR--VTGVDISPEMLELAREKAPREGLT------FVVGDAEDlpFPDNSFDLVLSSEVLHHVE 73

                          90
                  ....*....|....*..
gi 1225045451 255 DPVGAAAHVRRSLKPQG 271
Cdd:pfam08241  74 DPERALREIARVLKPGG 90
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 150-285 1.62e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 62.06  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 150 YAANLVSQWIPALEGIEPLLKRGARVADVGCGHGASTLLMAQAYPesSFVGFDYHAPSIERARETARKAGVDDEKRlrfq 229
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERALLNVRFDQFDEQEA---- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1225045451 230 vasakDFPGENYDLVAVFDCLHDMGDPVGAAAHVRRSLKPQGTWMIVEPFANDRLE 285
Cdd:pfam13489  75 -----AVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEAD 125
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
174-342 3.09e-11

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 62.43  E-value: 3.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451  174 RVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGVDDEKRLRFQVASAKDFPGeNYDLVAVFDCLHDM 253
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPD-TYDLVFGFEVIHHI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451  254 GDPVGAAAHVRRSLKPQGTWMIVEPFANDRLEDNInPVGRVFYSASSFICTPASR-----------SQEVGLCLGAQAGE 322
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAIEH-EETTSYLVTREEWAELLARnnlrvvegvdaSLEIANFLYDPGFE 159

                          170       180
                   ....*....|....*....|....*..
gi 1225045451  323 ARLREV-------VTQGGFSHFRRASE 342
Cdd:smart00828 160 DNLERLyqddldeVTKRHFRGIANLGK 186
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 159-281 1.16e-10

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 60.94  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 159 IPALEGIEPllkrGARVADVGCGHGASTLLMAQA-YPESSFVGFDYHAPSIERARETARKAGVDDekRLRFQVASAKD-F 236
Cdd:COG2519    83 IIARLDIFP----GARVLEAGTGSGALTLALARAvGPEGKVYSYERREDFAEIARKNLERFGLPD--NVELKLGDIREgI 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1225045451 237 PGENYDLVAVfdclhDMGDPVGAAAHVRRSLKPQGTWMIVEPFAN 281
Cdd:COG2519   157 DEGDVDAVFL-----DMPDPWEALEAVAKALKPGGVLVAYVPTVN 196
PRK08317 PRK08317
hypothetical protein; Provisional
 169-278 8.23e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 58.41  E-value: 8.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAY-PESSFVGFDYHAPSIERAREtaRKAGVDDEKRLRFQVASAKDFPGENYDLVA-- 245
Cdd:PRK08317   17 VQPGDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDADGLPFPDGSFDAVRsd 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1225045451 246 -VFDCLHdmgDPVGAAAHVRRSLKPQGTWMIVEP 278
Cdd:PRK08317   95 rVLQHLE---DPARALAEIARVLRPGGRVVVLDT 125
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
171-271 2.17e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.16  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 171 RGARVADVGCGHGASTLLMAQAYpeSSFVGFDYHAPSIERARETarkaGVDDekrlRFQVASAKDF--PGENYDLVAVFD 248
Cdd:COG4976    46 PFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREK----GVYD----RLLVADLADLaePDGRFDLIVAAD 115

                          90       100
                  ....*....|....*....|...
gi 1225045451 249 CLHDMGDPVGAAAHVRRSLKPQG 271
Cdd:COG4976   116 VLTYLGDLAAVFAGVARALKPGG 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 174-271 6.15e-08

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 50.12  E-value: 6.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 174 RVADVGCGHGASTLLMAQAYPEsSFVGFDYHAPSIERARETARKAGVDdekRLRFQVASAKDFP---GENYDLVAVFDCL 250
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA-RVTGVDISPVALELARKAAAALLAD---NVEVLKGDAEELPpeaDESFDVIISDPPL 76

                          90       100
                  ....*....|....*....|..
gi 1225045451 251 HD-MGDPVGAAAHVRRSLKPQG 271
Cdd:cd02440    77 HHlVEDLARFLEEARRLLKPGG 98
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 169-244 9.48e-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: 52.07  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGVDDekRLRFQVASAKDFP----GENYDLV 244
Cdd:COG4123    35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLED--RITVIHGDLKEFAaelpPGSFDLV 112
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 172-276 9.39e-07

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: 48.65  E-value: 9.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 172 GARVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGVDDekrLRFQVASA-KDFPGENYDLVAvfdC- 249
Cdd:COG2813    50 GGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN---VEVLWSDGlSGVPDGSFDLIL---Sn 123

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1225045451 250 --LHDMGDPVGAAAH-----VRRSLKPQGTWMIV 276
Cdd:COG2813   124 ppFHAGRAVDKEVAHaliadAARHLRPGGELWLV 157
PLN02244 PLN02244
tocopherol O-methyltransferase
 131-276 9.67e-07

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 50.13  E-value: 9.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 131 WHEHdaaLFHGterFFRPGY--AANLVSQwipaLEGIEPLL----------KRGARVADVGCGHGASTLLMAQAYpESSF 198
Cdd:PLN02244   76 WGEH---MHHG---YYDPGAsrGDHRQAQ----IRMIEESLawagvpdddeKRPKRIVDVGCGIGGSSRYLARKY-GANV 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 199 VGFDYHAPSIERARETARKAGVDDekRLRFQVASAKD--FPGENYDLVAVFDCLHDMGDPVGAAAHVRRSLKPQGTWMIV 276
Cdd:PLN02244  145 KGITLSPVQAARANALAAAQGLSD--KVSFQVADALNqpFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIV 222
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 177-221 1.04e-06

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 48.60  E-value: 1.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1225045451 177 DVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGVD 221
Cdd:COG0220    38 EIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLT 82
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 169-244 1.47e-06

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 47.87  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAYPESS-FVGFDYHAPSIERARETARKAGVDDekRLRFQVASA----KDFPGENYDL 243
Cdd:COG4122    14 LLGAKRILEIGTGTGYSTLWLARALPDDGrLTTIEIDPERAAIARENFARAGLAD--RIRLILGDAlevlPRLADGPFDL 91


                  .
gi 1225045451 244 V 244
Cdd:COG4122    92 V 92
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 162-276 3.78e-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: 46.43  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 162 LEGIEPLLKRgaRVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGVDDEKRLRFQVASakDFPGENY 241
Cdd:pfam05175  24 LEHLPKDLSG--KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYS--GVEDGKF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1225045451 242 DLVAVFDCLHDMGDPVGAAAH-----VRRSLKPQGTWMIV 276
Cdd:pfam05175 100 DLIISNPPFHAGLATTYNVAQrfiadAKRHLRPGGELWIV 139
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 178-275 4.14e-06

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 44.99  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 178 VGCGHGASTLLMAQAYPE---SSFVGFDYHaPSIERARETARKAGVDDekRLRFQVA----SAKDFPGENYDLVaVFDCL 250
Cdd:pfam13578   3 IGTYSGVSTLWLAAALRDnglGRLTAVDPD-PGAEEAGALLRKAGLDD--RVRLIVGdsreALPSLADGPIDLL-FIDGD 78

                          90       100
                  ....*....|....*....|....*
gi 1225045451 251 HDMGDPVGAAAHVRRSLKPQGTWMI 275
Cdd:pfam13578  79 HTYEAVLNDLELWLPRLAPGGVILF 103
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
 175-220 4.12e-05

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 43.89  E-value: 4.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1225045451 175 VADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGV 220
Cdd:TIGR00091  20 HLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGL 65
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 147-213 4.70e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 44.16  E-value: 4.70e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1225045451 147 RPgyAANLVSQwIPalegieplLKRGARVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARE 213
Cdd:PRK01683   18 RP--ARDLLAR-VP--------LENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARS 73
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 175-220 5.40e-05

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 43.05  E-value: 5.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1225045451 175 VADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERARETARKAGV 220
Cdd:pfam02390   5 FLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGL 50
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
162-244 5.86e-05

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 44.01  E-value: 5.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 162 LEGIEPLLKRGARVADVGCGHG-----ASTLLMAQAYpessfvGFDYHAPSIERARETARKAGVDDekrlRFQVASAKDF 236
Cdd:COG2264   139 LEALEKLLKPGKTVLDVGCGSGilaiaAAKLGAKRVL------AVDIDPVAVEAARENAELNGVED----RIEVVLGDLL 208


                  ....*...
gi 1225045451 237 PGENYDLV 244
Cdd:COG2264   209 EDGPYDLV 216
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 170-244 3.11e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 41.98  E-value: 3.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1225045451 170 KRGARVADVGCGHGASTLLMAQAYPESSFVGFDYHAPSIERAREtarkAGVDdekrlrFQVASAKDF-PGENYDLV 244
Cdd:PRK14103   28 ERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARE----RGVD------ARTGDVRDWkPKPDTDVV 93
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 169-277 3.17e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 41.68  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQAYPES-SFVGFDYHAPSIERARETARKAGVDDekRLRFQVASAKD--FPGENYDLVA 245
Cdd:PRK00216   49 VRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSG--NVEFVQGDAEAlpFPDNSFDAVT 126

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1225045451 246 VFDCLHDMGDPVGAAAHVRRSLKPQGTWMIVE 277
Cdd:PRK00216  127 IAFGLRNVPDIDKALREMYRVLKPGGRLVILE 158
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 143-275 3.70e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 42.05  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 143 ERFFRPGYAAN----LVSQWIPALEgieplLKRGARVADVGCGHGASTLLMAQAYpESSFVGFDYHAPSIERARETA--R 216
Cdd:PLN02336  239 ERVFGEGFVSTggleTTKEFVDKLD-----LKPGQKVLDVGCGIGGGDFYMAENF-DVHVVGIDLSVNMISFALERAigR 312

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1225045451 217 KAGVDdekrlrFQVA--SAKDFPGENYDLVAVFDCLHDMGDPVGAAAHVRRSLKPQGTWMI 275
Cdd:PLN02336  313 KCSVE------FEVAdcTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLI 367
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 158-250 4.32e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.36  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 158 WIPALegiePLLKrGARVADVGCGHGASTLLMAQAypessfvGFDYHAPSI-----ERARETARKAGVDDekRLRFQVAS 232
Cdd:PRK07580   55 WLPAD----GDLT-GLRILDAGCGVGSLSIPLARR-------GAKVVASDIspqmvEEARERAPEAGLAG--NITFEVGD 120

                          90
                  ....*....|....*...
gi 1225045451 233 AKDFPGEnYDLVAVFDCL 250
Cdd:PRK07580  121 LESLLGR-FDTVVCLDVL 137
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 169-272 1.78e-03

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 39.40  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225045451 169 LKRGARVADVGCGHGA-STLLMAQAYPESSFVGFDYHAPSIERARETARKAGVDDEKRLRFQVASAKDFPGE-NYDLVAV 246
Cdd:pfam08704  38 LRPGSVVCESGTGSGSlSHAIIRTVAPTGHLFTFEFHEQRADKAREEFREHGIDQLVTVTHRDVCKEGFLTEvSGKADAV 117

                          90       100
                  ....*....|....*....|....*.
gi 1225045451 247 FdclHDMGDPVGAAAHVRRSLKPQGT 272
Cdd:pfam08704 118 F---LDLPSPWEAVPHAWKALKVEGG 140
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
169-227 3.75e-03

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 38.12  E-value: 3.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1225045451 169 LKRGARVADVGCGHGASTLLMAQaypessFVGFDYHAPSIERARETARKAgvddEKRLR 227
Cdd:pfam01135  71 LKPGMRVLEIGSGSGYLTACFAR------MVGEVGRVVSIEHIPELVEIA----RRNLE 119
 
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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